lactoferrin has been researched along with Amyloidosis* in 16 studies
3 review(s) available for lactoferrin and Amyloidosis
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[Amyloidosis of the seminal vesicles: a local condition with no systemic impact].
Localised seminal vesicle amyloidosis is relatively infrequent and we present 9 additional cases.. and methods: Those 9 cases were retrospectively retrieved from 803 radical prostatectomies performed between 1995 and 2000 for prostatic adenocarcinoma. In each case, the type of amyloidosis was characterised by immunohistochemistry. Information regarding a possible concurrent disease or prior hormone therapy has been obtained.. The prevalence of amyloidosis of seminal vesicles is lower in our study (1.1%) than in unselected autopsy cases. The prevalence of amyloidosis in patients exposed to prior hormone therapy (LHRH agonist and anti-androgen) was 2% while it reached only 0.9% in those who received no hormone therapy (p>0.3). No patient had systemic amyloidosis and all cases were of non A-A type. Lactoferrin, a glycoprotein produced by normal seminal vesicles, was detected in more than a half of them (5/9).. No association was found between the occurrence of seminal vesicle amyloidosis and occurrence of a prostatic adenocarcinoma, corcomitant systemic disease or exposure to prior hormone therapy. Seminal vesicle amyloidosis is a localised condition without systemic involvement and amyloid deposition is composed mostly of lactoferrin. Topics: Adenocarcinoma; Adult; Aged; Amyloid; Amyloidosis; Androgen Antagonists; Antineoplastic Agents, Hormonal; Combined Modality Therapy; France; Genital Diseases, Male; Gonadotropin-Releasing Hormone; Humans; Lactoferrin; Male; Middle Aged; Neoadjuvant Therapy; Prevalence; Prostatectomy; Prostatic Neoplasms; Retrospective Studies; Seminal Vesicles | 2004 |
[A case of corneal lactoferrin amyloidosis secondary to trichiasis].
A case of corneal lactoferrin amyloidosis secondary to trichiasis is reported.. A 30-year-old male suffered from trichiasis with an elevated gray whitish lesion just under the center of the cornea in his right eye. The lesion had an irregular surface.. We excised the corneal lesion, and studied the excised corneal lesion morphologically.. The deposit observed just under the corneal epithelial layer was positive for Congo red staining, and showed dichroism under polarizing microscopy. The deposit also showed a immunoreactivity against anti-human lactoferrin antibody.. The morphological study proved that the deposits under the corneal lesion were derived from lactoferrin. Long term injury of the corneal surface by trichiasis may lead to the deposition and structural changes of lactoferrin originating from tears. Topics: Adult; Amyloidosis; Corneal Diseases; Eyelashes; Humans; Lactoferrin; Male | 2003 |
[Analyses of pathogenesis and therapeutic approaches for hereditary amyloidosis].
Amyloidosis is a disorder of protein metabolism in which normally soluble autologous proteins are deposited in tissues as abnormal insoluble fibrils, causing structural and functional disruptions. We have recently identified the novel localized amyloidosis accompanied by trichiasis. The precursor protein of amyloid deposits was mutated lactoferrin and all the patients had lactoferrin Glu561Asp. The disease was classified hereditary amyloidosis whose risk factor is trichiasis. We examined the therapeutic possibilities for mutated transthyretin(ATTR) related familial amyloidotic polyneurpathy(FAP), one of the systemic amyloidoses. Cr3+ suppressed amyloid formation by stabilizing ATTR structure in vitro. BSB is a useful new diagnostic tool to detect amyloid deposits both in in vitro and in vivo and may have therapeutic potential for preventing amyloid deposition. Gene therapy using single-stranded oligonuclotides(SSOs) may become a promising tool for therapy instead of liver transplantation. SSOs with athrocollagen effectively replaced the TTR gene both in vitro and in vivo. Topics: Amyloidosis; Chromium; DNA, Single-Stranded; Genetic Therapy; Humans; Lactoferrin; Liver Transplantation; Mutation; Oligonucleotides; Prealbumin; Styrenes | 2003 |
13 other study(ies) available for lactoferrin and Amyloidosis
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Detection of Secondary Corneal Lactoferrin Amyloidosis Based on Histologic Biopsies Combined with Mass Spectrometry: A Case Report.
Amyloidosis is characterized by systemic or local deposition of amyloid fibrils outside organs and tissues. Amyloidosis is rarely seen on cornea. A 30-year-old woman patient had had trichiasis in both eyes for 8 years. Trichiasis was observed, which touched the cornea. Slit lamp microscopy showed white gelatinous droplet-like eminences and trichiasis in the lower cornea of the right eye. Optical coherence tomography showed that the lesion involved most of the cornea. Hematoxylin and eosin staining showed that most of the stroma stained red, with scattered inflammatory cells. High expression of lactoferrin was detected by mass spectrometry, and the case was diagnosed as secondary corneal lactoferrin amyloidosis in the right eye. Topics: Adult; Amyloidosis; Amyloidosis, Familial; Biopsy; Cornea; Corneal Dystrophies, Hereditary; Eyelashes; Female; Humans; Lactoferrin; Mass Spectrometry; Trichiasis | 2022 |
Lactotransferrin-Related Breast Amyloidosis: Report of a First Case.
Breast amyloidosis is a rare condition which is mostly associated with hematological disorders or hereditary genetic disorders. Imaging findings of breast amyloidosis can mimic malignancy, which often leads to biopsy or excision of the lesion. Here, we presented a case of localized lactotransferrin-related breast amyloidosis in an elderly female patient. Histologic examination revealed extensive involvement of breast lobules by amorphous amyloid materials, with attenuation of lobular structures and prominent calcifications. Positive immunostains for myoepithelial cells helped to exclude the possibility of invasive carcinoma. The patient had no hematologic malignancy besides immunoglobulin G lambda monoclonal gammopathy of undetermined significance. Mass spectrometry of the breast amyloid identified lactotransferrin and no immunoglobulin or its light chain. On follow-up, the patient showed no recurrence of the breast lesion after local excision nor showed other systematic comorbidities, indicating the benign nature of the lesion. This first report of lactotransferrin-related amyloidosis may represent a special type of localized breast amyloidosis that has no correlation with systematic disorders. Topics: Amyloidosis; Biomarkers; Breast Diseases; Diagnosis, Differential; Female; Humans; Lactoferrin; Middle Aged | 2022 |
Lactoferrin amyloid presenting as a mural nodule in a pancreatic cystic lesion prompting pancreatoduodenectomy: a case report.
Amyloid deposition in pancreas is rare. Lactoferrin amyloid deposition has not been reported in pancreas, till date. Presence of enhancing mural nodule in a cyst on imaging is a worrisome feature for malignancy, and warrants surgical resection in a surgically fit candidate, as per Fukuoka guidelines for management of cystic lesions in pancreas.. We report a case of localized amyloidosis presenting as a mural nodule in a 1.6 cm cyst located in the head of pancreas, which led to pancreatoduodenectomy in a 69 year old woman. Histological evaluation revealed a simple mucinous cyst with localized lactoferrin amyloid deposition corresponding to the mural nodule identified on imaging.. We report the first case of localized lactoferrin amyloid deposition in pancreas that presented as a mural nodule in a cystic lesion and prompted pancreatoduodenectomy. This unique case illustrates that on rare occasion mural nodule in a cyst can be benign. It adds amyloid deposition to the differential diagnosis of mural nodules in pancreatic cystic lesions seen on imaging. Topics: Aged; Amyloidosis; Female; Humans; Lactoferrin; Pancreas; Pancreatic Cyst; Pancreatic Neoplasms; Pancreaticoduodenectomy | 2021 |
A case of spheroid-type localized lactoferrin amyloidosis in the bronchus.
We report a case of localized bronchial lactoferrin amyloidosis. A 47-year-old man presented with a complaint of persistent dry cough for two months. Chest computed-tomography revealed a calcification shadow of the right main bronchus; hence, a biopsy was performed, showing layered spheroid-type eosinophilic deposits in the bronchial wall. These deposits were positive for Congo red staining, exhibiting apple-green birefringence under polarized light. In addition, an electron microscopic examination demonstrated that this layered structure was formed by very thin cord-like amyloid deposits. By proteomics analysis using liquid chromatography-tandem mass spectrometry and immunohistochemistry, we confirmed that the deposited amyloid was composed of lactoferrin. While lactoferrin is known to be a precursor protein of localized corneal and seminal vesicle amyloidosis, localized lactoferrin amyloidosis of the bronchus has not been reported in the English literature. Our pathological findings suggested that localized lactoferrin amyloidosis may be caused by long-term tissue damage, and the characteristic spheroid-type appearance is thought to be associated with unique, thin cord-like amyloid deposits. Topics: Amyloidosis; Biopsy; Bronchi; Bronchial Diseases; Bronchoscopy; Calcinosis; Chromatography, Liquid; Humans; Immunohistochemistry; Lactoferrin; Male; Middle Aged; Proteomics; Tandem Mass Spectrometry; Tomography, X-Ray Computed | 2019 |
Classification of secondary corneal amyloidosis and involvement of lactoferrin.
To classify secondary corneal amyloidosis (SCA) by its clinical appearance, to analyze the demographics of the patients, and to determine the involvement of lactoferrin.. Retrospective, observational, noncomparative, multicenter study.. Twenty-nine eyes of 29 patients diagnosed with SCA by corneal specialists at 9 ophthalmologic institutions in Japan were studied.. The clinical appearance of SCA was determined by slit-lamp biomicroscopy and was classified into 3 types. The demographics of the patients, for example, age, gender, and the duration of the basic disease (trichiasis, keratoconus, and unknown), were determined for each clinical type. Surgically excised tissues were stained with Congo red and antilactoferrin antibody. The postoperative prognosis also was determined.. Clinical appearance of the 3 types of SCA, along with the gender, age, and duration of the basic diseases were determined.. Classification of SCA into 3 types based on clinical appearance found 21 cases with gelatinous drop-like dystrophy (GDLD)-like appearance (GDLD type), 3 cases with lattice corneal dystrophy (LCD)-like appearance (LCD type), and 5 cases with the combined type. Patients with the GDLD type were younger (average age: 40.9 years for the GDLD type, 74.3 years for the LCD type, and 46.8 years for the combined type), predominantly women (85.7% for the GDLD type, 33.3% for the LCD type, and 60% for the combined type), and had the basic disease over a longer time (average duration: 22.1 years for the GDLD type, 14.0 for the LCD type, and 11.4 for the combined type). The distribution of the basic diseases (trichiasis vs. keratoconus vs. unknown) was not significantly different for each type. Surgical treatments, for example, phototherapeutic keratectomy, lamellar keratoplasty, and simple keratectomy, resulted in a good resolution in all surgically treated cases. One subject dropped out of the study. Spontaneous resolution was seen in one subject after epilation of the cilia. Amorphous materials in the excised tissues showed positive staining results by Congo red and by antilactoferrin antibody.. Secondary corneal amyloidosis can be classified into 3 clinical types based on its clinical appearance. Larger numbers of females and lactoferrin expression were seen in all 3 types.. The author(s) have no proprietary or commercial interest in any materials discussed in this article. Topics: Adult; Aged; Amyloidosis; Corneal Diseases; Female; Humans; Immunoenzyme Techniques; Lactoferrin; Male; Microscopy; Microscopy, Polarization; Middle Aged; Retrospective Studies | 2013 |
Characterization of localized seminal vesicle amyloidosis causing hemospermia: an analysis using immunohistochemistry and magnetic resonance imaging.
We evaluated the characteristics of seminal vesicle amyloidosis (SVA) associated with hemospermia by immunohistochemistry and magnetic resonance imaging (MRI) as well as the clinical course of hemospermia.. Of 56 patients with hemospermia 12 underwent transperineal biopsy of the seminal vesicle under transrectal ultrasound monitoring. SVA was proved in 4 men 48 to 59 years old by histological and immunohistochemical examinations of specimens obtained by biopsy. Two men presented with the first episode of hemospermia and 2 presented with recurrent hemospermia. MRI at 1.5 Tesla was performed while hemospermia persisted and after its resolution. Patients were followed for 10 to 86 months with regard to the duration of hemospermia, the time of its resolution and its recurrence.. Amyloid deposits in the subepithelial tissue of the seminal vesicles were permanganate sensitive, and positive for lactoferrin and the amyloid P component but negative for amyloid A protein, lambda and kappa chains, and beta2-microglobulin. The seminal vesicles with obvious intravesicular hemorrhage on needle puncture were hyperintense on T1-weighted images. After hemospermia resolution T1-weighted images became diffusely hypointense. T2-weighted images were of low intensity, representing amyloid deposits. Hemospermia resolved spontaneously in all patients in an average of 14 months. Although disease recurred in 1 patient after 8 months of resolution, it disappeared after 11 months of recurrence.. Localized SVA with hemospermia shows hypointensity on T2-weighted MRI. Hemospermia is spontaneously resolved with the transition from hyperintense to hypointense T1-weighted MRI. Topics: Amyloid; Amyloidosis; beta 2-Microglobulin; Biopsy, Needle; Blood; Epithelium; Follow-Up Studies; Genital Diseases, Male; Hemorrhage; Humans; Immunoglobulin kappa-Chains; Immunoglobulin lambda-Chains; Immunohistochemistry; Lactoferrin; Magnetic Resonance Imaging; Male; Middle Aged; Recurrence; Remission, Spontaneous; Semen; Seminal Vesicles; Serum Amyloid A Protein; Serum Amyloid P-Component; Ultrasonography, Interventional | 2005 |
Lactoferrin Glu561Asp facilitates secondary amyloidosis in the cornea.
To elucidate the pathogenic mechanism of amyloid formation in corneal amyloidosis with trichiasis.. Ophthalmological examination was performed in nine patients to determine secondary corneal amyloidosis with trichiasis. Congo red staining and immunohistochemistry using anti-human lactoferrin antibody were used for biopsied corneal samples. For genetic analyses, single strand conformation polymorphism (SSCP), direct DNA sequence analysis, and polymerase chain reaction (PCR) induced mutation restriction analysis (IMRA) were employed to detect lactoferrin gene polymorphism.. All patients had had trichiasis at least for 1 year, and all amyloid-like deposits were found in one eye with trichiasis. Ophthalmological examination revealed that eight patients showed gelatinous type of amyloid deposition and one showed lattice type of amyloid deposition. Studies of biopsied corneal samples with Congo red stain revealed positive staining just under the corneal epithelial cells. Immunoreactivity of anti-human lactoferrin antibodies was recognised in all tissues with positive Congo red staining. Lactoferrin gene analysis revealed that seven patients were heterozygotic and two were homozygotic for lactoferrin Glu561Asp. The frequency of the polymorphism in the patients was significantly different from that in 56 healthy control subjects.. Lactoferrin Glu561Asp is a key polymorphism related to facilitating amyloid formation in corneal amyloidosis with trichiasis. Topics: Adolescent; Adult; Aged; Aged, 80 and over; Amyloidosis; Child; Congo Red; Corneal Diseases; Eyelashes; Eyelid Diseases; Female; Gene Frequency; Genetic Predisposition to Disease; Hair Diseases; Humans; Immunoenzyme Techniques; Lactoferrin; Male; Middle Aged; Polymerase Chain Reaction; Polymorphism, Single-Stranded Conformational; Sequence Analysis, DNA | 2005 |
A novel localized amyloidosis associated with lactoferrin in the cornea.
We report a novel localized amyloidosis associated with lactoferrin. To elucidate the precursor protein of corneal amyloidosis associated with trichiasis, we analyzed amyloid deposits from three patients by histopathology and biochemistry. Amyloid deposits showed immunoreactivity, confirmed by electron microscopy, for only anti-human lactoferrin antibody. Electrophoresis of amyloid fibrils revealed lactoferrin with and without sugar chains; N-terminal sequence analysis revealed full-length lactoferrin and a truncated tripeptide of N-terminal amino acids, Gly-Arg-Arg. Carboxymethylated wild-type lactoferrin formed amyloid fibrils in vitro. Lactoferrin gene analysis in the three patients revealed a Glu561Asp mutation in all of the patients and a compound heterozygote of Ala11Thr and Glu561Asp mutations in one patient. A heterozygotic Glu561Asp mutation appeared in 44.8% of healthy Japanese volunteers, suggesting that the mutation may not be an essential mutation for amyloid formation (p = 0.104). Results thus suggest that lactoferrin is this precursor protein. Topics: Adult; Aged; Amyloid; Amyloidosis; Cornea; Corneal Diseases; Electrophoresis, Polyacrylamide Gel; Eyelashes; Eyelid Diseases; Female; Heterozygote; Humans; Immunohistochemistry; Lactoferrin; Male; Molecular Sequence Data; Point Mutation | 2002 |
[Heterogeneity of seminal vesicle amyloid. Immunohistochemical detection of lactoferrin and amyloid of the prealbumin-transthyretin type].
Localized depositions of amyloid in the seminal vesicles may occur in elderly men. Earlier immunohistochemical studies have failed to identify immunoreactivity of known amyloid material. In this autopsy study, all seminal vesicles of males older than 50 years were histologically examined to determine incidence and phenotype of seminal vesicle amyloidosis. Seven out of 50 patients (14%) showed depositions of amyloid in the seminal vesicles. These amyloid depositions as well as one additional case were characterized histochemically, immunohistochemically and electronmicroscopically. All but two of these patients (75%) showed simultaneously amyloid depositions in the heart. Lactoferrin immunoreactivity was found in 6 patients (75%). Lactoferrin is an iron-binding, bacteriostatic glycoprotein, which is produced in the seminal vesicles. Four patients with lactoferrin positive amyloid in seminal vesicle showed different amyloid depositions in the heart (immunoglobulin light chain amyloid AL-lambda). Two cases (25%) showed the same amyloid type in heart and seminal vesicles (prealbumin-transthyretin type amyloid). Our study shows that most amyloidoses of the seminal vesicles are organ-limited depositions of lactoferrin. These forms of localized amyloidosis have to be separated from senile systemic amyloidosis with seminal vesicle involvement. Topics: Aged; Aged, 80 and over; Amyloid; Amyloidosis; Epithelium; Humans; Immunoenzyme Techniques; Lactoferrin; Male; Microscopy, Electron; Middle Aged; Prealbumin; Seminal Vesicles | 1998 |
Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene.
Because corneal tissue with familial subepithelial corneal amyloidosis (FSCA; gelatinous drop-like dystrophy of the cornea) contains lactoferrin the possibility that the FSCA gene was the human lactoferrin (hLF) gene was investigated. Due to contradictory published information we also mapped the hLF gene.. We mapped the hLF gene using a genomic clone of the entire hLF gene as a probe by fluorescence in situ hybridization (FISH). Utilizing PCR primers that are specific to the hLF gene, we also mapped the hLF via radiation somatic cell hybrid analysis. Linkage of the FSCA gene to the hLF gene was evaluated by genetic linkage analysis using polymorphic markers within and in the vicinity of the hLF gene.. The hLF gene mapped to the short arm of chromosome 3 at 3p21. Linkage analysis using polymorphic markers for hLF and haplotype analysis of the 3p21 loci indicates that the FSCA gene is not linked to the 3p21 locus.. The gene for FSCA is not the hLF gene in these families. Topics: Amyloidosis; Chromosome Mapping; Chromosomes, Human, Pair 3; Corneal Dystrophies, Hereditary; Female; Genetic Linkage; Haplotypes; Humans; In Situ Hybridization, Fluorescence; Lactoferrin; Male; Pedigree; Polymorphism, Genetic; Polymorphism, Single-Stranded Conformational | 1998 |
Familial subepithelial corneal amyloidosis--a lactoferrin-related amyloidosis.
To isolate the protein that collects in increased amounts beneath the corneal epithelium in familial subepithelial corneal amyloidosis (FSCA), also known as gelatinous droplike corneal dystrophy, and to identify it by N-terminal amino acid sequencing.. Peptides resulting from pepsin digestion of a unique protein isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis from frozen tissue from two corneas with FSCA were purified by high-pressure liquid chromatography followed by protein sequence analysis. The protein was identified by amino acid sequencing, Western blotting, and immunohistochemistry.. A protein was identified in two corneas with FSCA that was not present in normal corneas or in corneas with other disorders. The amino acid sequences of two peptides derived from this protein were identical to portions of lactoferrin. The unique protein reacted with rabbit antihuman lactoferrin after Western blotting. The presence of lactoferrin in the amyloid within affected corneas was confirmed using the immunoperoxidase method on formalin-fixed, paraffin-embedded tissue sections and lactoferrin antiserum.. Corneal tissue with FSCA contains lactoferrin, and this is the first form of amyloidosis found to be associated with this protein. Because lactoferrin is a product of lacrimal glands, the corneal lactoferrin may be derived from the tears. Because the gene for lactoferrin is on chromosome 3 (3q21-q23), this locus is a potential site for the FSCA gene. Topics: Adolescent; Amino Acid Sequence; Amyloid; Amyloidosis; Blotting, Western; Chromatography, High Pressure Liquid; Corneal Diseases; Electrophoresis, Polyacrylamide Gel; Epithelium, Corneal; Eye Proteins; Humans; Immunoenzyme Techniques; Lactoferrin; Male; Molecular Sequence Data | 1997 |
Localized amyloidosis of the seminal vesicle: identification of lactoferrin immunoreactivity in the amyloid material.
Three specimens of localized amyloidosis of the seminal vesicle surgically removed for prostatic cancer were immunohistochemically analyzed to clarify the nature of the permanganate-sensitive congophilic subepithelial deposition. A variety of known amyloidogenic substances and secretory products in the seminal fluid were screened using the indirect immunoperoxidase method. In addition to reactivities with antibodies to amyloid P component and human seminal plasma, the amyloid material was immunoreactive for lactoferrin using a rabbit antiserum and two of three mouse monoclonal antibodies. All the antibodies labeled some of the normal seminal vesicle epithelial cells for this ironbinding, bacteriostatic glycoprotein. In the prostate without accompanying amyloid deposition, a considerable proportion of the glandular epithelium and secretory material were positive for lactoferrin. Pre-embedding immunoelectron microscopy showed lactoferrin immunoreactivity on the amyloid fibrils. Focal staining of the amyloid for gross cystic disease fluid protein-15 was also observed in two lesions. These findings strongly suggest that lactoferrin is the major constituent in localized senile amyloidosis of the seminal vesicle. Topics: Aged; Amyloidosis; Antibodies, Monoclonal; Humans; Immunohistochemistry; Lactoferrin; Male; Seminal Vesicles | 1996 |
Evaluation of a new polyamide membrane (Polyflux 130) in high-flux dialysis.
Removal of beta 2-microglobulin has become a major objective of dialysis therapy. The present study was performed to evaluate both compatibility and elimination capacity for beta 2-microglobulin of a newly developed high-flux polyamide membrane (Polyflux 130) during hemodialysis. The degree of leukopenia was moderate (-22%) and comparable with Polysulfone 600 (-25%). C3a desarg generation had a tendency to be lower with the Polyflux 130 membrane, and C5a desarg formation was identical with both types of membranes. As for degranulation of polymorphonuclear leukocytes, plasma elastase levels increased by 209% with Polyflux 130 and by 160% with Polysulfone 600 membranes. Likewise, plasma lactoferrin values rose during hemodialysis by 233% (Polyflux 130) and 160% (Polysulfone 600). The differences between membranes, however, were statistically not significant. There was a sharp drop in the serum levels of beta 2-microglobulin during dialysis with both membranes (Polyflux 130: -46%; Polysulfone 600: -48%). Accordingly, sieving coefficients were calculated to be 0.77 +/- 0.06 for Polyflux 130 and 0.80 +/- 0.06 for the Polysulfone 600 membrane. Both membranes were capable to remove large quantities of beta 2-microglobulin, amounting to 235 +/- 11 and 250 +/- 10 mg/4 h of dialysis for Polyflux 130 and Polysulfone 600, respectively. Topics: Adult; Amyloidosis; beta 2-Microglobulin; Cellulose; Complement Activation; Evaluation Studies as Topic; Humans; Lactoferrin; Leukopenia; Membranes, Artificial; Middle Aged; Nylons; Pancreatic Elastase; Polymers; Renal Dialysis; Sulfones; Uremia | 1990 |