elastin and Multiple-Myeloma

Cutis laxa acquisita is a rare disorder that affects collagen and elastin metabolism. The cause is unknown. Characteristic features include sagging and laxity of the skin, as well as involvement of the lungs, heart, gastrointestinal system, and urogenital tract. Three cases of cutis laxa acquisita have been reported in association with multiple myeloma. Due to the rarity of these disorders, a linkage has been postulated. The clinical and histologic data from the fourth case of cutis laxa acquisita associated with multiple myeloma were compared to the three other cases previously reported in the literature. The relationship between acquired cutis laxa and multiple myeloma is unclear, with only one case revealing possible immune-mediated elastin destruction via IgG immunoglobulin bound to dermal elastin fibers on immunofluoresence examination. No pattern in the clinical courses of the disorder can be seen on review of the four cases with coincident disease. We hypothesize that cutis laxa acquisita represents a paraneoplastic process of multiple myeloma, given the rarity of these diseases. Further investigation is necessary to determine the underlying linkage between these disorders. We suggest that serum and urine protein electrophoresis results be obtained in patients presenting with cutis laxa acquisita to screen for multiple myeloma given this association.

Topics: Antineoplastic Agents; Biomarkers; Cutis Laxa; Elastin; Humans; Male; Middle Aged; Multiple Myeloma

The identification and use of antibodies dominate the biologic, clinical diagnostic, and therapeutic landscapes. In particular, antibodies have become essential tools in a variety of protein analytical experiments and to study the disposition of biologic therapeutics. One emerging class of peptide biologics is known as the elastin-like polypeptides (ELPs), which are repetitive protein polymers inspired by human tropoelastin. A major limitation in the clinical translation of ELP biologics has been a lack of a monoclonal antibody (mAb) to characterize their identity during expression. To facilitate these studies, we successfully generated a new mAb that is specific toward ELPs and ELP fusion proteins. A purified antibody was evaluated in an ELISA, western blotting, and immunofluorescence assay. The optimal anti-ELP mAb proved to be highly reactive and specific toward ELPs. Moreover, they were able to detect ELPs with a variety of aliphatic guest residues. ELPs phase-separate in response to heating; furthermore, when incubated at a great excess of ELPs, the anti-ELP mAb partially blocks phase separation. These findings are direct evidence that novel murine mAbs can be raised against purified ELPs. This new reagent will enable purification, experimental detection, and characterization of these biopolymers.

Topics: Animals; Antibodies, Monoclonal; Antibody Formation; Biopolymers; Elastin; Female; Immunization; Mice; Mice, Inbred BALB C; Multiple Myeloma; Peptides