Macaque MDC family of proteins: sequence analysis, tissue distribution and processing in the male reproductive tract

Frayne, Jan; Jury, Jenny A.; Barker, Helen L.; Perry, Anthony C.F.; Jones, Roy; Hall, Len

doi:10.1093/molehr/4.5.429

Cited by 32 publications

(13 citation statements)

References 45 publications

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“…Some of these modifications result from very specific proteolytic processing leading to the disappearance or the redistribution of proteins among the different domains [18,19]. Examples of these proteolytically transformed compounds are the different members of the ADAMs (i.e., a disintegrin and metalloprotease domain) family in rodents and monkeys (for reviews see [20][21][22][23]), the rat sperm CE9 antigen [24] and hyaluronidase (pH20/ 2B1) [25], the boar 135-kDa mannosidase [26], and the germinal form of angiotensin converting enzyme (ACE) in several domestic mammals [27].…”

Section: Introductionmentioning

confidence: 99%

Comparison, Characterization, and Identification of Proteases and Protease Inhibitors in Epididymal Fluids of Domestic Mammals. Matrix Metalloproteinases Are Major Fluid Gelatinases1

Métayer

Dacheux

et al. 2002

Biology of Reproduction

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The testicular and epididymal fluids of ram, boar, and stallion were analyzed by means of one-dimensional and two-dimensional gelatin gel zymography. Five main gelatinolytic bands were revealed in the ram and at least seven were observed in the boar and stallion. These proteolytic bands showed regionalized distribution throughout the organs. The two main proteolytic activities at around 54-66 kDa retrieved in all three species were inhibited by EDTA and phenanthroline, indicating that they were metallo-dependent enzymes. The activity of some of the low-molecular-weight gelatinases was also decreased by EDTA, whereas others were inhibited by serine protease inhibitors. One of the main proteases at 60-62 kDa from the caput fluid of the stallion and the ram was N-terminal sequenced; in both cases, high sequence homology was found with the N-terminal of the matrix-metalloproteinase-2 pro-form (pro-MMP-2). Antibodies against MMP-2, MMP-3, and MMP-9 gelatinases confirmed the regional distribution in the fluids of pre -, pro-, active, or degraded forms of these metalloproteases in all three species. We also observed the presence of acrosin in epididymal fluids, which was probably released by dead spermatozoa, but this enzyme did not explain all the serine protease activity. Moreover, the majority of this enzyme is bound to the protease inhibitor alpha(2)-macroglobulin, which is present in the fluids of all three species. TIMP-2, a potent inhibitor of MMPs, was present in the fluid of the caput regions in the ram and boar, and in the caput and caudal fluids of the stallion. This study demonstrated that similar types of proteases and inhibitors are regionally distributed in the epididymal fluids of three domestic species, suggesting an identical role in the sperm maturation process, the plasticity of this organ, or both.

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Section: Introductionmentioning

confidence: 99%

Comparison, Characterization, and Identification of Proteases and Protease Inhibitors in Epididymal Fluids of Domestic Mammals. Matrix Metalloproteinases Are Major Fluid Gelatinases1

Métayer

Dacheux

et al. 2002

Biology of Reproduction

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“…Little is known about the activity or functions of the other 13 ADAMs with a catalytic site consensus sequence, except that seven of them appear to be expressed predominantly in the testis, suggesting a role in sperm function [4,[15][16][17][18][19][20][21][22][23]. ADAMs harbouring a catalytic site that are known to be expressed in somatic cells include MDC9 [24], ADAM10\KUZ [8,9,25], ADAM8\ MS2 [26], ADAM12\meltrin α [27], MDC15 [28][29][30], ADAM17\ TACE (tumour necrosis factor converting enzyme) [10,11] and ADAM19\meltrin β [31,32].…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28

Howard

Maciewicz

Blobel

2000

Biochemical Journal

101

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The metalloprotease disintegrins are a family of membraneanchored glycoproteins with diverse functions in fertilization, myoblast fusion, neurogenesis and protein ectodomain shedding. Here we report a cDNA sequence, encoding a metalloprotease disintegrin, termed ADAM28 (' a disintegrin and metalloprotease 28 '), which was cloned from mouse lung. From protein sequence comparisons, ADAM28 is more closely related to snake venom metalloproteases (SVMPs) than to other ADAMs, and hence may cleave similar substrates to SVMPs, perhaps including components of the extracellular matrix. Northern blot analysis of selected mouse tissues revealed that ADAM28 is expressed highly and in alternatively spliced forms in the epididymis, suggesting a possible role in sperm maturation, and at lower levels in lung. The intracellular maturation of ADAM28 expressed in COS-7 cells resembles that of other ADAMs, in that ADAM28 is made as a precursor and processed to a mature form in a late Golgi

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“…Processing of several sperm proteins during the epididymal sojourn has been reported. This includes the proteolytic cleavage of fertilin b (Phelps Lum and Blobel, 1997;Hunnicutt et al, 1997) and other MDC (metalloproteinase-and disintegrin-like, cysteine-rich) proteins in monkey sperm (Frayne et al, 1998), rat CE9 (Petruszak et al, 1991), mannosidase (Tulsiani et al, 1995), and 2B1 (PH20, Jones et al, 1996), and partial deglycosylation of PH20 in the mouse (Deng et al, 1999). On the other hand, since there are high glycosyltransferase and glycosidase activities in the epididymis, further glycosylation or modi®cation of glycoproteins can occur (Tulsiani et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Maturational changes of the CD52-like epididymal glycoprotein on cynomolgus monkey sperm and their apparent reversal in capacitation conditions

Yeung¹,

Schröter²,

Kirchhoff³

et al. 2000

Mol. Reprod. Dev.

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A major epididymal secretory protein in men has a colinear cDNA sequence with lymphocyte CD52, a sialylated glycoprotein. Immunostaining and flow cytometric detection of cynomolgus monkey sperm CD52 during epididymal maturation showed increases from 20 to 85% stained sperm from the caput to the corpus with staining intensities doubled. Freshly prepared cauda sperm showed only 10% staining while they markedly increased in percentage and intensity of staining upon incubation at 37°C under capacitating conditions, but not at 4°C. Western blotting of proteins from fresh cauda sperm revealed no less antigen than corpus sperm. Staining of ejaculated sperm exhibited similar increases during incubation. Further washing with a high salt medium before staining to remove any electrostatically‐bound molecules masking the antigen showed no effect. Incubation‐induced increases in antigen binding were accelerated by the addition of neuraminidase (0.25 and 0.5 U/ml), but not affected by the sialyl residue‐rich fetuin (5 mg/ml) competing for any endogenous neuraminidase. There were no concomitant decreases in the staining of sialic acid residues during capacitation‐incubation. These findings suggest a cryptic antigen epitope site as a consequence of sperm maturation and subsequent re‐exposure under capacitation conditions, but not due to the removal of sialic acid residues by endogenous neuraminidase. Involvement of endogenous proteases was also ruled out, as incubation in the presence of protease inhibitors did not hinder the increases but resulted in a dose‐dependent enhancement in staining, suggesting some protease‐sensitive unmasking process. In conclusion, the monkey epididymal secreted CD52 on sperm underwent changes in antigenic characteristics during sperm maturation which were reversed under capacitation conditions. Mol. Reprod. Dev. 57:280–289, 2000. © 2000 Wiley‐Liss, Inc.

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Macaque MDC family of proteins: sequence analysis, tissue distribution and processing in the male reproductive tract

Cited by 32 publications

References 45 publications

Comparison, Characterization, and Identification of Proteases and Protease Inhibitors in Epididymal Fluids of Domestic Mammals. Matrix Metalloproteinases Are Major Fluid Gelatinases1

Comparison, Characterization, and Identification of Proteases and Protease Inhibitors in Epididymal Fluids of Domestic Mammals. Matrix Metalloproteinases Are Major Fluid Gelatinases1

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28

Maturational changes of the CD52-like epididymal glycoprotein on cynomolgus monkey sperm and their apparent reversal in capacitation conditions

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