Semenogelin I is the amyloidogenic protein in senile seminal vesicles

R. P. Linke, R. Joswig, C. L. Murphy, S. Wang, H. Zhou, U. Gross, C. B. Röcken, W. B.J. Nathrath, P. Westermark, D. Weiss, A. Solomon

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The protein of origin in senile amyloid of the seminal vesicles has been identified in this study. Amyloid fibrils were isolated from frozen seminal vesicles in a pure form. Immunochemical and chemical studies revealed that a major polypeptide of 13 KDa represents an N-terminal fragment of semenogelin I (SgI). Similar polypeptides of SgI were isolated from formalin-fixed seminal vesicles containing amyloid. Although it had been reported previously that this material contained lactoferrin and it was suggested that lactoferrin was the protein of origin, the results of our studies revealed that lactoferrin was not present in significant amounts in pure amyloid fibrils. Since semenogelin I was identified as the protein of origin of senile seminal vesicle amyloid, we provisionally designate this entity as ASgI.

Original languageEnglish (US)
Title of host publicationAmyloid and Amyloidosis
PublisherCRC Press
Pages471-473
Number of pages3
ISBN (Electronic)9781420037494
ISBN (Print)0849335345, 9780849335341
StatePublished - Jan 1 2004

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Amyloidogenic Proteins
Seminal Vesicles
Amyloid
Lactoferrin
Peptides
Proteins
Formaldehyde

All Science Journal Classification (ASJC) codes

  • Medicine(all)
  • Immunology and Microbiology(all)
  • Neuroscience(all)

Cite this

Linke, R. P., Joswig, R., Murphy, C. L., Wang, S., Zhou, H., Gross, U., ... Solomon, A. (2004). Semenogelin I is the amyloidogenic protein in senile seminal vesicles. In Amyloid and Amyloidosis (pp. 471-473). CRC Press.

Semenogelin I is the amyloidogenic protein in senile seminal vesicles. / Linke, R. P.; Joswig, R.; Murphy, C. L.; Wang, S.; Zhou, H.; Gross, U.; Röcken, C. B.; Nathrath, W. B.J.; Westermark, P.; Weiss, D.; Solomon, A.

Amyloid and Amyloidosis. CRC Press, 2004. p. 471-473.

Research output: Chapter in Book/Report/Conference proceedingChapter

Linke, RP, Joswig, R, Murphy, CL, Wang, S, Zhou, H, Gross, U, Röcken, CB, Nathrath, WBJ, Westermark, P, Weiss, D & Solomon, A 2004, Semenogelin I is the amyloidogenic protein in senile seminal vesicles. in Amyloid and Amyloidosis. CRC Press, pp. 471-473.
Linke RP, Joswig R, Murphy CL, Wang S, Zhou H, Gross U et al. Semenogelin I is the amyloidogenic protein in senile seminal vesicles. In Amyloid and Amyloidosis. CRC Press. 2004. p. 471-473
Linke, R. P. ; Joswig, R. ; Murphy, C. L. ; Wang, S. ; Zhou, H. ; Gross, U. ; Röcken, C. B. ; Nathrath, W. B.J. ; Westermark, P. ; Weiss, D. ; Solomon, A. / Semenogelin I is the amyloidogenic protein in senile seminal vesicles. Amyloid and Amyloidosis. CRC Press, 2004. pp. 471-473
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AU - Linke, R. P.

AU - Joswig, R.

AU - Murphy, C. L.

AU - Wang, S.

AU - Zhou, H.

AU - Gross, U.

AU - Röcken, C. B.

AU - Nathrath, W. B.J.

AU - Westermark, P.

AU - Weiss, D.

AU - Solomon, A.

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AB - The protein of origin in senile amyloid of the seminal vesicles has been identified in this study. Amyloid fibrils were isolated from frozen seminal vesicles in a pure form. Immunochemical and chemical studies revealed that a major polypeptide of 13 KDa represents an N-terminal fragment of semenogelin I (SgI). Similar polypeptides of SgI were isolated from formalin-fixed seminal vesicles containing amyloid. Although it had been reported previously that this material contained lactoferrin and it was suggested that lactoferrin was the protein of origin, the results of our studies revealed that lactoferrin was not present in significant amounts in pure amyloid fibrils. Since semenogelin I was identified as the protein of origin of senile seminal vesicle amyloid, we provisionally designate this entity as ASgI.

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