Heterogeneity of<i>β</i><sub>2</sub>-Microglobulin in Human Urine

Tanahashi, Nobuyasu; Watanabe, Yutaka; Yamada, Fujizo

doi:10.1080/00021369.1979.10863689

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“…Furthermore, immunoblots confirm that fibrils are composed of dimers, tetramers, and higher polymers of p2m, only partially dissociated in buffer used for two-dimensional gels. The observed heterogeneity is consistent with observations reported by others for f32m in urine (23) and colostrum (35), but its significance is unclear. Since human P2m is coded for by a single gene (27) and does not contain carbohydrate (1), one may assume that it reflects posttranslational changes or modifications (e.g., deamidation) introduced during purification.…”

Section: Arg-val-asn-his-val-thr-leu-ser-gln-pro-lys-ile-val-lys-trp-supporting

confidence: 82%

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Gorevic¹,

Muñoz²,

Casey³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

159

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Systemic amyloidosis with a predilection for bone and synovium may complicate the course of patients on long-term hemodialysis. This form of amyloidosis can be typed as distinct from other amyloid diseases by using small tissue samples obtained by bone biopsy and at postmortem. Immunoblot analysis of two-dimensional gels of partially solubilized amyloid fibrils established that tissue deposits are composed of monomers, dimers, and higher polymers of beta 2-microglobulin (beta 2m) and that amyloid P component was also present. Anti-beta 2m antiserum recognized fibrils, as shown by immunoelectron microscopy. Purified monomer isolated from dissociated fibrils yielded peptides corresponding to the entire known sequence of beta 2m. Virtually all serum beta 2m, as well as that present in tissue fluid bathing amyloid fibrils, was monomeric. Hemodialysis-related amyloidosis is an example of a deposition disease occurring in hemodialysis patients. We have shown conclusively that, in this amyloid disease, polymerization of an intact normal serum protein to a fibrillar configuration may occur without proteolysis. We propose the designation A beta 2m for this form of amyloid fibril subunit protein.

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Section: Arg-val-asn-his-val-thr-leu-ser-gln-pro-lys-ile-val-lys-trp-supporting

confidence: 82%

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Gorevic¹,

Muñoz²,

Casey³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

159

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Heterogeneity ofβ₂-Microglobulin in Human Urine

Cited by 1 publication

References 1 publication

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

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Heterogeneity ofβ2-Microglobulin in Human Urine

Cited by 1 publication

References 1 publication

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

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Heterogeneity ofβ₂-Microglobulin in Human Urine