acid-phosphatase and Melanoma

Serum antibodies are valuable source of information on the health state of an organism. The profiles of serum antibody reactivity can be generated by using a high throughput sequencing of peptide-coding DNA from combinatorial random peptide phage display libraries selected for binding to serum antibodies. Here we demonstrate that the targets of immune response, which are recognized by serum antibodies directed against sequential epitopes, can be identified using the serum antibody repertoire profiles generated by high throughput sequencing. We developed an algorithm to filter the results of the protein database BLAST search for selected peptides to distinguish real antigens recognized by serum antibodies from irrelevant proteins retrieved randomly. When we used this algorithm to analyze serum antibodies from mice immunized with human protein, we were able to identify the protein used for immunizations among the top candidate antigens. When we analyzed human serum sample from the metastatic melanoma patient, the recombinant protein, corresponding to the top candidate from the list generated using the algorithm, was recognized by antibodies from metastatic melanoma serum on the western blot, thus confirming that the method can identify autoantigens recognized by serum antibodies. We demonstrated also that our unbiased method of looking at the repertoire of serum antibodies reveals quantitative information on the epitope composition of the targets of immune response. A method for deciphering information contained in the serum antibody repertoire profiles may help to identify autoantibodies that can be used for diagnosing and monitoring autoimmune diseases or malignancies.

Topics: Acid Phosphatase; Algorithms; Amino Acid Sequence; Animals; Antibodies; Blotting, Western; Computer Simulation; Databases, Protein; Enzyme-Linked Immunosorbent Assay; Epitope Mapping; HEK293 Cells; High-Throughput Nucleotide Sequencing; Humans; Immunization; Melanoma; Mice; Prostate-Specific Antigen; Software

Clinical and genomic evidence suggests that the metastatic potential of a primary tumor may be dictated by prometastatic events that have additional oncogenic capability. To test this "deterministic" hypothesis, we adopted a comparative oncogenomics-guided function-based strategy involving: (1) comparison of global transcriptomes of two genetically engineered mouse models with contrasting metastatic potential, (2) genomic and transcriptomic profiles of human melanoma, (3) functional genetic screen for enhancers of cell invasion, and (4) evidence of expression selection in human melanoma tissues. This integrated effort identified six genes that are potently proinvasive and oncogenic. Furthermore, we show that one such gene, ACP5, confers spontaneous metastasis in vivo, engages a key pathway governing metastasis, and is prognostic in human primary melanomas.

Topics: Acid Phosphatase; Animals; Cell Lineage; Conserved Sequence; Evolution, Molecular; Gene Expression Profiling; Gene Expression Regulation, Neoplastic; Genome; Humans; Isoenzymes; Kaplan-Meier Estimate; Melanoma; Mice; Neoplasm Invasiveness; Neoplasm Metastasis; Neoplasm Staging; Oncogenes; Phosphorylation; Reproducibility of Results; Skin Neoplasms; Tartrate-Resistant Acid Phosphatase; Tissue Array Analysis

Tartrate-resistant acid phosphatase (TRAP) is a metalloprotein enzyme that belongs to the acid phosphatases and is known to be expressed by osteoclasts. It has already been investigated as a marker of bone metastases in cancer patients. In this study, which examined the value of serum TRAP concentrations as a marker of bone disease in breast cancer patients, we observed high concentrations of TRAP even in patients without bone metastases. To elucidate this phenomenon, we examined the expression of TRAP in breast cancer cells and the cells of several other malignancies.. TRAP concentrations in the serum of tumor patients were determined by ELISA. The expression of TRAP in breast, ovarian, and cervical cancer and malignant melanoma was analyzed by immunohistochemistry. RT-PCR and immunocytology were used to evaluate TRAP expression in cultured tumor cells.. A marked increase in serum TRAP concentrations was observed in patients with breast and ovarian cancer, regardless of the presence or absence of bone disease. TRAP expression was found in breast and ovarian cancers and malignant melanoma, while cervical cancer showed only minimal expression of TRAP. Expression of TRAP was absent in benign tissue or was much less marked than in the corresponding malignant tissue. TRAP expression was also demonstrated in cultured primary cancer cells and in commercially available cell lines.. Overexpression of TRAP was detected in the cells of various different tumors. TRAP might be useful as a marker of progression of malignant disease. It could also be a potential target for future cancer therapies.

Topics: Acid Phosphatase; Breast Neoplasms; Control Groups; Enzyme-Linked Immunosorbent Assay; Female; Gene Expression; Humans; Immunohistochemistry; Isoenzymes; Melanoma; Ovarian Neoplasms; Reverse Transcriptase Polymerase Chain Reaction; Tartrate-Resistant Acid Phosphatase; Tumor Cells, Cultured; Up-Regulation

The effects of a third-generation bisphosphonate, YM175 (disodium dihydrogen (cycloheptylamino)-methylene-1,1-bisphosphonate), on bone resorption induced by a metastatic human melanoma cell line (A375) were investigated morphologically using an experimental model of bone metastases in nude mice. An injection of A375 in the left cardiac ventricle produced multiple osteolytic lesions. Then, 4 weeks after the cell injection, we administrated YM175 (1 mg/kg) intravenously once and sacrificed the animals 3 days later. On histochemical observation, there was a layer of stromal cells with numerous mononuclear and multinucleated tartrate-resistant acid phosphatase (TRAPase)-positive cells in the untreated control group. In contrast, this layer was extensively reduced in most areas, and only a few TRAPase-positive cells were seen around tumor nests and on the bone surface in the experimental group. Most of the TRAPase-positive cells were stained only weakly and/or homogeneously, and there was little evidence of cell polarity. Some of them were vacuolated. Ultrastructurally, they were round and devoid of ruffled borders and clear zones. The findings suggest that YM175 decreases the number and activity of osteoclasts. In addition, a few showed the morphology of cell death, which seemed to be one of the reasons leading to the decrease of osteoclasts. There was no substantial change in the morphological relationships or ultrastructure of osteoclast precursor cells, stromal cells, extracellular matrices, and tumor cells between the experimental and the control groups. In the experimental group, the distribution of extracellular matrices (heparan sulfate proteoglycan and fibronectin) was less conspicuous, but the localization of osteotropic cytokines (interleukin-6 and prostaglandin E2) was essentially similar to that of the control group. The cause leading to the decrease of osteoclast precursor cells remains to be clarified. In conclusion, YM175 inhibits bone resorption induced by tumor, by decreasing the activity of mature osteoclasts and possibly affecting the production of osteoclast precursor cells.

Topics: Acid Phosphatase; Animals; Biomarkers, Tumor; Bone Neoplasms; Bone Resorption; Diphosphonates; Humans; Immunohistochemistry; Isoenzymes; Male; Melanoma; Mice; Mice, Nude; Neoplasm Transplantation; Tartrate-Resistant Acid Phosphatase; Tumor Cells, Cultured

The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.

Topics: Acid Phosphatase; Amino Acid Sequence; Antigens, Neoplasm; Binding Sites; Cell Line, Transformed; Hepacivirus; Hepatitis B virus; Herpesvirus 4, Human; HIV; HLA-A2 Antigen; Humans; Male; Melanoma; Melanoma-Specific Antigens; Molecular Sequence Data; Neoplasm Proteins; Oligopeptides; Papillomaviridae; Peptide Fragments; Prostate; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Receptor, ErbB-2; Sequence Homology, Amino Acid; Tumor Suppressor Protein p53; Viral Proteins

A histochemical study of alpha-D-mannosidase revealed that normal human melanocytes (resting state, activated, lentigo simplex) exhibit either no or just detectable activity, as do melanocytes in the initial phase of lentigo maligna. Junctional, or occasionally zone A naevocytes displayed a very low enzyme activity. On the other hand, melanocytes in the initial stage of neoplastic transformation (dysplastic naevi, advanced stage of lentigo maligna) and also melanoma cells in disorders of low malignant potential (initial naevogenic melanoma, superficial spreading melanoma) displayed a high activity uniformly throughout the cell population. In the malignant forms (nodular melanoma, recurrences, metastases), the enzyme activity was remarkably heterogeneous, suggesting a breakdown of uniformity during malignant transformation. The significance of alpha-mannosidase activity induction in the course of melanocyte neoplastic transformation is not clear at present. The results of biochemical assays suggest that the lysosomal isoenzyme is mainly responsible. Other lysosomal enzymes, and dehydrogenases studied concomitantly, did not display any comparable phenomena of induction or similar behaviour. However, the results of a comparison of alpha-mannosidase with the melanocyte reference enzyme tyrosinase suggested activity patterns in the enzyme pair which may provide a better insight into the biochemical differentiation of human melanocytes in neoplastic disorders. The possible relationship of alpha-mannosidase to melanogenesis is also discussed.

Topics: Acid Phosphatase; Alkaline Phosphatase; alpha-Mannosidase; Carboxylesterase; Carboxylic Ester Hydrolases; Glucuronidase; Histocytochemistry; Humans; Mannosidases; Melanoma; Monophenol Monooxygenase; Nevus, Pigmented; Oxidoreductases; Skin Neoplasms

The diameter of the fibrils in the normal vitreous cortex at the ora serrata of human eyes was found to range from 10.8 to 12.4 nm. There is no significant increase in thickness with age. Periodic cross-striation typical for collagen could be demonstrated by microdensitometry. In senile eyes, secondary lateral aggregations of the fibrils are a common factor, usually in proximity to disintegrating cells. Disintegrating cells in the vitreous cortex were already observable in childhood. They were more often seen with increasing age. In a pathological case, acid phosphatase could be demonstrated both within the vitreous fibrocytes and in the extracellular space, released from disintegrating cells. Fibrils and segments of banded material were observed within pits and invaginations, and in intracytoplasmic channels and vacuoles of the aged vitreous fibrocytes. Linear aggregations of ruthenium red-positive material were seen at the surface and within invaginations of the same cells. The findings are interpreted as an indication for phagocytosis and--or secretion of collagen by the vitreous fibrocytes even in senile eyes.

Topics: Acid Phosphatase; Actin Cytoskeleton; Adult; Aged; Aging; Collagen; Eye Neoplasms; Female; Fibroblasts; Humans; Infant; Male; Melanoma; Microscopy, Electron; Middle Aged; Retinoblastoma; Uveal Neoplasms; Vacuoles; Vitreous Body

Topics: Acid Phosphatase; Circadian Rhythm; Glucuronidase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Melanoma; Skin Neoplasms

An immunoperoxidase technique to detect prostatic-specific acid phosphatase (PSAP) was used on specimens from 98 cases of prostatic carcinoma that were graded by both the Gleason and the Mostofi systems, to see if tumor grade correlated with amount of PSAP seen in tissue. Most tumors showed strong, diffuse cytoplasmic staining; no significant difference was seen among the various grades. Other than focal, weak staining of renal tubular epithelium, the antibody to PSAP gave uniformly negative results with a variety of normal and neoplastic tissues. In light of the great sensitivity and specificity of this technique, it potential applications include diagnosis of poorly differentiated prostatic malignant neoplasms, whether primary or metastatic.

Topics: Acid Phosphatase; Adenocarcinoma; Carcinoma, Intraductal, Noninfiltrating; Carcinoma, Squamous Cell; Humans; Immunoenzyme Techniques; Male; Melanoma; Neoplasm Staging; Prostatic Neoplasms; Wilms Tumor

In solid s.c. tumors of a variant of the murine B16 melanoma with high metastatic potential (B16F10), there was a 2- to 7-fold elevation of lysosomal cathepsin B activity when compared to the B16F1 variant with low metastatic potential. The highest activities (based on either protein or DNA) of cathepsin B were found in tumors of less than 1 g. When B16F1 and B16F10 melanoma variants were grown in tissue culture, the metastatic differential in cathepsin B activity was lost as the cells were subcultured. However, this differential in cathepsin B activity could be restored by reestablishing the cultured cells as s.c. tumors. The activities of four other lysosomal enzymes (cathepsin D, beta-N-acetylglucosaminidase, beta-glucuronidase, and acid phosphatase) showed little evidence of a positive correlation with the metastatic potential of the B16 melanoma variants. Eighty to 90% of cathepsin B activity has been localized to a fraction containing viable tumor cells which was isolated by centrifugal elutriation. In contrast, only 50% of cathepsin D activity was in the viable tumor cell fraction, and from 30 to 70% of beta-N-acetylglucosaminidase, beta-glucuronidase, and acid phosphatase. Elevated levels of cathepsin B in the high metastatic B16F10 variant are consistent with the idea that cathepsin B may play a direct or a regulatory role in tumor metastasis.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Cathepsin B; Cathepsin D; Cathepsins; Cell Line; Glucuronidase; Lysosomes; Melanoma; Mice; Mutation; Neoplasm Metastasis; Neoplasm Transplantation; Neoplasms, Experimental

Purified plasma membranes were obtained from five transplantable human tumors, a grade IV astrocytoma, an oat cell carcinoma, and three melanomas. Plasma membrane fractions were isolated from tumor homogenates by differential and discontinuous sucrose gradient centrifugation. Determination of enzyme activities indicated that the plasma membranes were enriched 10- to 20-fold with respect to 5'-nucleotidase, nicotinamide adenine dinucleotide glycohydrolase, Mg2+-activated nucleoside triphosphatase, and sialic acid. Specific activities of nearly all the enzymes varied with the individual tumors, even among tumors of the same type, i.e., the melanomas. Electron micrographs of the plasma membrane fractions showed smooth single-membrane vesicles with slight contamination by lysosomes. Therefore, these membranes are suitable for comparative biochemical studies and for the preparation of tumor-specific monoclonal antibodies. Plasma membranes from all five tumors contained very high Mg2+-adenosine triphosphatase (ATPase) activities. The Na+-K+-ATPase was a minor component of the total ATPase of these membranes (less than 30%). The major component was an ATPase exhibiting similar activity toward several nucleoside triphosphates. The activity of such a nucleoside triphosphatase has been correlated with tumorigenicity in cultured liver epithelial cells. The nucleoside triphosphatase of the plasma membranes of astrocytoma and oat cell carcinoma was stimulated from 50 to 1005 by concanavalin A, whereas ATPase of the melanoma plasma membranes was not or only slightly stimulated. The different response to concanavalin A could be due to differences in the ATPase molecules of the individual tumors or to the different environment of the ATPase.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Ca(2+) Mg(2+)-ATPase; Carcinoma, Small Cell; Cell Membrane; Glioblastoma; Humans; Melanoma; Mice; Mice, Nude; NAD+ Nucleosidase; NADH Dehydrogenase; Neoplasm Transplantation; Neoplasms, Experimental; Nucleotidases; Sialic Acids; Transplantation, Heterologous

A murine melanoma variant (B16-F10ir6), resistant to lymphocytic cytolysis, has been shown previously to produce lower numbers of tumor nodules in the lung of C57BL/6J mice following i.v. inoculations. These differences found in tumor implantation and lymphocyte recognition may be due to changes in surface properties of this cell line. Therefore, membrane-bound sialic acid (released by Vibrio cholerae neuraminidase treatment), ectosialyltransferase activity, and total cellular glycosidase levels were measured in this cell line and compared with levels in its parent melanoma tumor cell line, B16-F10, which was selected for its enhanced ability to form tumor nodules. The results of these studies indicate a correlation between the degree of lung implantation and the amount of tumor cell sialic acid accessible to neuraminidase cleavage, tumor cell surface sialyltransferase activity, and several cellular glycosidase activities. These results are consistent with the idea that membrane structural changes in the glycocalyx may account for the ability of a tumor cell to implant and metastasize.

Topics: Acid Phosphatase; Animals; Cell Line; Cell Membrane; Glycoside Hydrolases; Lung Neoplasms; Melanoma; Mice; Mice, Inbred C57BL; Neoplasm Transplantation; Neoplasms, Experimental; Sialic Acids; Sialyltransferases; Transferases

Topics: Acid Phosphatase; Enzyme Activation; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Lymphocyte Activation; Lymphocytes; Melanoma; Skin Neoplasms; Succinate Dehydrogenase

A considerable increase in activity of the following enzymes: succinate dehydrogenase (SDH), lactate dehydrogenase (LDH), beta-hydrogenase (beta-HBDH), cytochrome oxidase (CO), and acid phosphatase (AP) was found in lymph nodes lymphocytes after 1 week of malignant melanoma passage in golden hamster (Mesocricetus auratus Waterhouse). The peripheral blood lymphocytes displayed, too, an increase in activity of all the enzymes mentioned except beta-HBDH and SDH. After 3 weeks of the melanoma growth, the animals affected showed a considerable decrease in activity of all the enzymes studied both in the lymph nodes and in the peripheral blood. The increase in enzymatic activity during the initial phase of tumour growth may be a manifestation of biological activation of the cellular defence of lymphocytes. On the other hand, the decrease in the activity seen at the advanced phase of the disease speaks for an impaired immune response.

Topics: Acid Phosphatase; Animals; Cricetinae; Electron Transport Complex IV; Female; Hydroxybutyrate Dehydrogenase; L-Lactate Dehydrogenase; Lymph Nodes; Lymphocytes; Male; Melanoma; Mesocricetus; Neoplasms, Experimental; Skin Neoplasms; Succinate Dehydrogenase

Activity of arylsulphatase, beta-glucuronidase, cathepsin D, and acid phosphatase in the homogenates of melanotic and amelanotic melanoma was determined. The activity of these enzymes is higher in melanotic than in amelanotic melanoma. Respective values for melanotic and amelanotic tumours are: arylsulphatase 10,78 +/- 3,20, and 1,45 +/- 0,66 micron 4-nitrocatechole/mg protein/hr; beta-glucuronidase 11,10 +/- 1,40, and 9,98 +/- 1,35 micron phenolphthalein/mg protein/hr; cathepsin D 4,24 +/- 1,37, and 3,26 +/- 0,73 micron tyrosine/mg protein/hr; acid phosphatase 230 +/- 22, and 180 +/- 25 micron p-nitrophenol/mg protein/hr. These differences are statistically significant. The increased activity of the lysosomal enzymes in melantoic melanoma probably depends on the occurrence of an higher number of lysosomes in tissues containing melanins.

Topics: Acid Phosphatase; Animals; Arylsulfatases; Cathepsins; Cricetinae; Glucuronidase; Hydrolases; Lysosomes; Male; Melanoma; Mesocricetus; Neoplasm Transplantation; Neoplasms, Experimental

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Child, Preschool; Eye Neoplasms; Female; Glioma; Humans; Male; Melanoma; Middle Aged; Mitochondria, Muscle; Oculomotor Muscles; Retinoblastoma

Cell lines were established from three hamster melanomas. One was a spontaneous melanotic tumour which lost its ability to produce pigment. Two were induced with DMBA (9.10 dimethyl 1,2-benz/a/anthracene). One of these was pigmented. The two amelanotic lines (CHT-1 and 2) produced highly malignant amelanotic tumours after reimplantation of tissue culture cells. Electron microscopy showed that melanin forming organelles were absent. Tyrosinase activity was also absent. The line established from the pigmented tumour (CHT-8) retained its pigment production for the first seven transfers. Cells from these cultures produced slow growing pigmented tumours. Cells from the 7th to the 35th transfer, a period of 28 weeks, failed to produce tumours but cells from the 36th and subsequent transfers produced slow growing amelanotic tumours. The change in tumorigenicity was not related to changes in the growth rate of the cells in vitro: this remained constant after the 11th transfer generation. Tyrosinase activity and a whole range of melanin forming organelles were present in cells of transfers 1 to 7 but absent from subsequent transfers. Type A and H virus particles were present in the two amelanotic cell lines, CHT-1 and 2. Although the two amelanotic lines produced highly malignant tumours the loss of a differentiated character--melanin production--was not invariably associated with increased malignancy. Three cell lines should provide a good system for studying the relationship between tumour differentiation and growth.

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cell Line; Cricetinae; Culture Techniques; Histocytochemistry; Melanoma; Neoplasms, Experimental; Pigmentation

We report the findings on clinicopathologic examination of three patients with balloon cell melanoma of the choroid. Ophthalmoscopically, all three had small, slowly progressive tumors at the posterior pole, with an encircling yellow halo. With fluorescein angiography, the yellow halo showed fluorescence similar to the remainder of the tumor, thus differentiating this substance from lipofuscin pigment, drusen and exudates. Light microscopy demonstrated prominent balloon cells which were most numerous at the tumor margins. These cells showed variable melanin pigmentation and were negative for lipid, acid mucopolysaccharide, and glycogen. Special enzyme studies (lactic dehydrogenase, succinic dehydrogenase, acid phosphatase, beta glucoronidase and aminopeptidase) demonstrated some similarity to melanocytic cells. Electron microscopy revealed premelanosomes and complex melanosomes in the cytoplasm of balloon cells without evidence of significant lipid.

Topics: Acid Phosphatase; Adult; Aminopeptidases; Choroid Neoplasms; Female; Fluorescein Angiography; Humans; Melanoma; Middle Aged; Oxidoreductases; Succinates

By means of histochemical methods (gel-film incubation-media) superficial spreading melanoma, nodular melanoma and lentigo maligna melanoma are investigated. The result of this examination is that with regard to their enzyme spectra, the nodular melanoma and the nodular part of the superficial spreading melanoma are very similar. Glucose-6-phosphate dehydrogenase shows the strongest enzyme reaction, followed by succinate dehydrogenase and lactate dehydrogenase. The beta-hydroxybutyrate dehydrogenase reaction is always weak. The reaction of acid phosphatase is between negative and weakly positive. Significant differences, however, are observed in lentigo maligna and in lentigo maligna melanoma. In both, the strongest formazan deposits are seen with succinate dehydrogenase, sometimes also with lactate dehydrogenase. The glucose-6-phosphate dehydrogenase reaction, however, is sometimes considerably weaker. In the case of lentigo maligna melanoma, the activity of beta-hydroxybutyrate dehydrogenase often is increased, and acid phosphatase also shows higher reactions than in the other melanomas. These differences in the enzyme pattern correspond to the different biological behavior of the tumours. The enzymatical and biological characteristics of lentigo maligna melanoma possibly derive more from the characteristics of the tumour itself which are not dependent on the area.

Topics: Acid Phosphatase; Esterases; Formazans; Glucosephosphate Dehydrogenase; Humans; Hydroxybutyrate Dehydrogenase; L-Lactate Dehydrogenase; Melanoma; Monophenol Monooxygenase; Nevus, Pigmented; Skin; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adolescent; Adult; Age Factors; Animals; Animals, Newborn; Antibodies, Neoplasm; Antigens, Neoplasm; Breast Neoplasms; Carcinoma; Cell Line; Child; Child, Preschool; Female; Fluorescent Antibody Technique; Hodgkin Disease; Humans; Infant; Leukemia; Lung Neoplasms; Lysosomes; Male; Melanoma; Microscopy, Electron; Middle Aged; Osteosarcoma; Rats; Sarcoma; Sex Factors; Statistics as Topic

Topics: Acid Phosphatase; Cells, Cultured; Dopamine beta-Hydroxylase; Glucosephosphate Dehydrogenase; Glucuronidase; Histocytochemistry; Humans; Melanoma; Microscopy, Electron; Skin Neoplasms; Tyrosine 3-Monooxygenase

Topics: Acid Phosphatase; Animals; Ascitic Fluid; Catechol Oxidase; Female; Lymphocyte Activation; Lymphocytes; Lysosomes; Macrophages; Melanocytes; Melanoma; Mice; Mice, Inbred BALB C; Microscopy, Electron; Neoplasm Transplantation; Neoplasms, Experimental; Organoids; Peritoneal Neoplasms; Phagocytosis; Radiation Chimera; Spleen; Thymidine; Tritium

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cathepsins; Chlorpromazine; Cricetinae; Liver; Male; Melanins; Melanoma; Neoplasm Transplantation; Neoplasms, Experimental; Proteins; Tyrosine

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Catechols; Cathepsins; Chloroquine; Cricetinae; Liver; Male; Melanins; Melanoma; Neoplasm Transplantation; Sulfatases; Tyrosine

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cathepsins; Cell Fractionation; Cyclic AMP; Female; Galactosidases; Glucuronidase; Hexosaminidases; Humans; Liver; Liver Neoplasms; Lysosomes; Melanins; Melanocytes; Melanoma; Mice; Mice, Inbred C57BL; Microscopy, Electron; Neoplasm Metastasis; Nucleosides; Organoids; Pigments, Biological

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Electron Transport Complex IV; Melanins; Melanocytes; Melanoma; Methods; Mice; Microscopy, Electron; Mitochondria; Monophenol Monooxygenase; Neoplasms, Experimental; Succinate Dehydrogenase; Ultracentrifugation

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Dihydrolipoamide Dehydrogenase; Glucosephosphate Dehydrogenase; Glutamate Dehydrogenase; Glycerolphosphate Dehydrogenase; Histocytochemistry; Humans; Isocitrate Dehydrogenase; L-Lactate Dehydrogenase; Malate Dehydrogenase; Melanoma; Nucleotidases; Oxidoreductases; Phosphogluconate Dehydrogenase; Phosphoric Monoester Hydrolases; Skin Neoplasms; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Chick Embryo; Deoxycholic Acid; Dihydroxyphenylalanine; In Vitro Techniques; Melanins; Melanocytes; Melanoma; Microscopy, Electron, Scanning; Rats; Retinal Pigments; Swine; Trypsin; Vibration

Topics: Abdominal Muscles; Acid Phosphatase; Aged; Cachexia; Carcinoma; Cathepsins; Female; Gallbladder Diseases; Gastrointestinal Neoplasms; Humans; Kidney Neoplasms; Liver Neoplasms; Lymphatic Metastasis; Lysosomes; Male; Melanoma; Middle Aged; Muscles; Neoplasms; Pancreatic Neoplasms; Peptic Ulcer

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cell Nucleus; Cricetinae; Cytoplasm; Cytoplasmic Granules; Glycerophosphates; Histocytochemistry; Kidney Neoplasms; Melanoma; Mice; Neoplasm Transplantation; Neoplasms, Experimental

Topics: Acetylesterase; Acid Phosphatase; Eosinophils; Esterases; Histocytochemistry; Humans; Lymphocytes; Macrophages; Mast Cells; Melanoma; Neutrophils; Peroxidases; Plasma Cells; Skin Neoplasms; Stilbenes; Thiocyanates

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Chemical Phenomena; Chemistry; Hydrolysis; In Vitro Techniques; Injections, Intraperitoneal; Melanoma; Mice; Mice, Inbred Strains; Phosphates; Phosphorus Isotopes; Radionuclide Imaging; Tissue Extracts

Topics: Acid Phosphatase; Alkaline Phosphatase; Bone Neoplasms; Bronchial Neoplasms; Carcinoma; Esterases; Glycerolphosphate Dehydrogenase; Histocytochemistry; Humans; Kidney Neoplasms; L-Lactate Dehydrogenase; Leukocytes; Lymphoma, Non-Hodgkin; Male; Melanoma; Neoplasms; Peroxidases; Pharyngeal Neoplasms; Rectal Neoplasms; Sarcoma; Staining and Labeling; Succinate Dehydrogenase; Testicular Neoplasms

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Calcium; Carcinoma, Ehrlich Tumor; Hydrolysis; Kidney; Liver; Lymphoma, Non-Hodgkin; Magnesium; Melanoma; Mice; Neoplasms, Experimental; Phosphates; Phosphoric Monoester Hydrolases; Polymers; Pyrophosphatases

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cathepsins; Glucuronidase; Liver; Lysosomes; Male; Melanoma; Mice; Neoplasm Proteins; Neoplasm Transplantation; Neoplasms, Experimental; Skin Neoplasms; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cricetinae; Histocytochemistry; Kidney Neoplasms; Melanoma; Mice; Neoplasm Transplantation; Neoplasms, Experimental

Topics: Acid Phosphatase; Amino Acids; Animals; Carbon Isotopes; Cathepsins; Culture Techniques; Dihydroxyphenylalanine; Glucuronidase; Liver; Lysosomes; Male; Melanins; Melanocytes; Melanoma; Mice; Mitochondria; Proteins; Skin Neoplasms

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cathepsins; Glucuronidase; Liver; Lysosomes; Melanoma; Mice; Microscopy, Electron; Neoplasm Transplantation; Neoplasms, Experimental; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Cricetinae; Cytoplasmic Granules; Dihydroxyphenylalanine; Endoplasmic Reticulum; Hemorrhage; Histocytochemistry; Melanins; Melanoma; Microscopy; Microscopy, Electron; Necrosis; Neoplasm Transplantation; Neoplasms, Experimental; Oncogenic Viruses; Ribosomes

Topics: Acid Phosphatase; Back; Cell Line; Chromatophores; Clone Cells; Culture Techniques; Dihydroxyphenylalanine; Foot; Golgi Apparatus; Humans; Lysosomes; Male; Melanocytes; Melanoma; Microscopy, Electron; Middle Aged; Mitochondria; Skin Neoplasms

Topics: Acid Phosphatase; Adenocarcinoma; Biopsy; Carcinoma, Bronchogenic; Carcinoma, Squamous Cell; Colorimetry; Esophageal Neoplasms; Female; Gastrointestinal Neoplasms; Hodgkin Disease; Humans; Intestinal Neoplasms; Laryngeal Neoplasms; Leucyl Aminopeptidase; Leukemia; Liver Neoplasms; Lymphoma, Non-Hodgkin; Male; Melanoma; Nasopharyngeal Neoplasms; Neoplasms; Pancreatic Neoplasms; Prostatic Neoplasms; Tongue Neoplasms; Urogenital Neoplasms

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cricetinae; Cytoplasm; Histocytochemistry; Humans; Lysosomes; Melanoma; Microscopy, Electron; Mitochondria; Necrosis; Neoplasms, Experimental; Skin; Skin Neoplasms

Topics: Acid Phosphatase; Animals; Histocytochemistry; Melanins; Melanoma; Mice; Microscopy, Electron; Neoplasms, Experimental

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Endoplasmic Reticulum; Golgi Apparatus; Histocytochemistry; Lysosomes; Melanoma; Mice; Microscopy, Electron; Neoplasms, Experimental; Phagocytosis; Phosphoric Monoester Hydrolases; Pyrophosphatases; Sulfatases

Topics: Acid Phosphatase; Animals; Chick Embryo; Epithelium; Histocytochemistry; Melanins; Melanoma; Mice; Microscopy, Electron; Neoplasms, Experimental; Retina; Retinal Pigments

Topics: Acid Phosphatase; Chromatophores; Humans; Lysosomes; Melanins; Melanoma; Phagocytosis; Tyrosine Decarboxylase

Topics: Acid Phosphatase; Alkaline Phosphatase; Choroid Neoplasms; Esterases; Humans; Melanoma

Topics: Acid Phosphatase; Alkaline Phosphatase; Cell Nucleus; Culture Techniques; DNA, Neoplasm; Glycogen; Histocytochemistry; Humans; Melanoma; RNA, Neoplasm; Skin Neoplasms; Succinate Dehydrogenase

Topics: Acid Phosphatase; Dihydroxyphenylalanine; Histocytochemistry; Humans; In Vitro Techniques; Melanins; Melanoma; Microscopy, Electron; Nevus, Pigmented; Phagocytosis; Skin; Tyrosine Decarboxylase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Chromatophores; In Vitro Techniques; Liver; Lysosomes; Melanins; Melanoma; Mice; Mitochondria; Neoplasms, Experimental; Radiation Effects; Rats; Succinate Dehydrogenase; Tyrosine Decarboxylase; Ultraviolet Rays

Topics: Acid Phosphatase; Adenocarcinoma; Carcinoma; Colonic Neoplasms; Coloring Agents; Diagnosis, Differential; Histocytochemistry; Histological Techniques; Humans; Lung Neoplasms; Lymphoma; Male; Melanoma; Neoplasm Metastasis; Neoplasms; Pathology; Prostatic Neoplasms; Rhabdomyosarcoma; Sarcoma; Staining and Labeling; Urinary Bladder Neoplasms

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Electron Transport Complex II; Melanins; Melanoma; Mice; Neoplasms; Neoplasms, Experimental; Research; Succinate Dehydrogenase; Tyrosine Decarboxylase; Ultraviolet Rays

Topics: Acid Phosphatase; Alkaline Phosphatase; Cholinesterases; Humans; In Vitro Techniques; Leucyl Aminopeptidase; Melanoma; Monoamine Oxidase; Nevus, Pigmented; Succinate Dehydrogenase; Tyrosine Decarboxylase