Nonpathological extracellular amyloid is present during normal epididymal sperm maturation

PLoS ONE

Volumn 7, Issue 5, 2012, Pages

  Whelly, Sandra ^a   Johnson, Seethal ^a   Powell, Jonathan ^a   Borchardt, Clinton ^a   Hastert, Mary Catherine ^b   Cornwall, Gail A ^a  

^a TEXAS TECH UNIVERSITY HEALTH SCIENCES CENTER SCHOOL OF MEDICINE   (United States)

^b TEXAS TECH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; CYSTATIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL ISOLATION; CONTROLLED STUDY; CYTOTOXICITY; EPIDIDYMIS; EXTRACELLULAR SPACE; MALE; MOUSE; NONHUMAN; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEMINIFEROUS TUBULE; SPERMATOZOON MATURATION; TRANSMISSION ELECTRON MICROSCOPY; X RAY DIFFRACTION;

AMYLOID; ANIMALS; EPIDIDYMIS; EXTRACELLULAR SPACE; MALE; MICE; MICE, 129 STRAIN; MICE, KNOCKOUT; SPERM MATURATION;

MAMMALIA;

EID: 84860523522     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036394     Document Type: Article

References (24)

1. Fowler DM, Koulov AV, Alory-Jost C, Marks MS, Balch WE, et al. (2006) Functional amyloid formation within mammalian tissue. Plos Biology 4: E6.
2. Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, et al. (2009) Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325: 328-332.
3. Demuro A, Mina E, Kayed R, Milton SC, Parker I, et al. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280: 11294-12300.
4. Gatti JL, Castella S, Dacheux F, Ecroyd H, Métayer S, et al. (2004) Post-testicular sperm environment and fertility. Animal Reprod Sci 82-83: 321-339.
5. Cornwall GA, Hann SR, (1995) Transient appearance of CRES protein during spermatogenesis and caput epididymal sperm maturation. Mol Reprod Dev 41: 37-46.
6. von Horsten HH, Johnson SS, SanFrancisco SK, Hastert MC, Whelly SM, et al. (2007) Oligomerization and transglutaminase cross-linking of the cystatin CRES in the mouse epididymal lumen: potential mechanism of extracellular quality control. J Biol Chem 282: 32912-32923.
7. Parent AD, Cornwall GA, Liu LY, Smith CE, Hermo L, (2011) Alterations in the testis and epididymis associated with loss of function of the cystatin-related epididymal spermatogenic (CRES) protein. J Androl 32: 444-463.
8. Palsdotti A, Snorradottir AO, Thorsteinsson L, (2006) Hereditary cystatin C amyloid angiopathy: genetic, clinical and pathological aspects. Brain Pathol 16: 55-59.
9. Puchtler H, Sweat F, (1965) Congo red as a stain for fluorescence microscopy of amyloid. J Histochem Cytochem 13: 693-694.
10. Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegen 2: 18.
11. Eanes ED, Glenner GG, (1968) X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 16: 673-677.
12. Loksztejn A, Dzwolak W, (2009) Noncooperative dimethyl sulfoxide-induced dissection of insulin fibrils: toward soluble building blocks of amyloid. Biochemistry 48: 4846-4851.
13. Lane A, Stanley CJ, Dealler S, Wilson SM, (2003) Polymeric ligands with specificity for aggregated prion proteins. Clin Chem 49: 1774-1775.
14. Sathasivam K, Lane A, Legleiter J, Warley A, Woodman B, et al. (2010) Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease. Human Mol Genetics 19: 65-78.
15. Cornwall GA, von Horsten HH, (2006) Sperm maturation in the epididymis: role of segment-specific microenvironments. In: Carrell D, editors. The Genetics of Male Infertility Humana Press pp. 211-231.
16. Turner TT, Johnston DS, Jelinsky SA, Tomsig JL, Finger JN, (2007) Segment boundaries of the adult rat epididymis limit interstitial signaling by potential paracrine factors and segments lose differential gene expression after efferent duct ligation. Asian J Androl 2007 9: 565-73.
17. Goldsbury C, Goldie K, Pellaud J, Seelig J, Frey P, et al. (2000) Amyloid fibril formation from full-length and fragments of amylin. J Struct Biol 130: 352-362.
18. Sabaté R, Lascu I, Saupe SJ, (2008) On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2. J Struct Biol 162: 387-396.
19. Cloe AL, Orgel JP, Sachleben JR, Tycko R, Meredith SC, (2011) The Japanese mutant Aβ (ΔE22-Aβ(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence: seeding of wild-type Aβ(1-40) into atypical fibrils by ΔE22-Aβ(1-39). Biochemistry 50: 2026-2039.
20. Glabe C, (2004) Conformation-dependent antibodies target diseases of protein misfolding. Trends in Biochem Sci 29: 542-546.
21. van Rooijen BD, Claessens MM, Subramaniam V, (2010) Membrane interactions of oligomeric α-synuclein: potential role in Parkinson's disease. Curr Protein Pept Sci 11: 334-342.
22. Leonhardt RM, Vigneron N, Rahner C, Cresswell P, (2011) Proprotein convertases process Pmel17 during secretion. J Biol Chem 286: 9321-9337.
23. Wahlbom M, Wang X, Lindstrom V, Carlemalm E, Jaskolski M, et al. (2007) Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping. J Biol Chem 282: 18318-18326.
24. Wang X, Chapman MR, (2008) Curli provide the template for understanding controlled amyloid propagation. Prion 2: 57-60.