Rat clusterin isolated from primary sertoli cell-enriched culture medium is sulfated glycoprotein-2 (SGP-2)

Cheng, C. Yan; Chen, Ching-Ling C.; Feng, Zhen; Marshall, A. David; Bardin, C. Wayne

doi:10.1016/s0006-291x(88)81099-4

Cited by 89 publications

(26 citation statements)

References 25 publications

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“…The secreted testicular protein is glycosylated and sulfated and demonstrates a lectinlike ability to aggregate cells in suspension (9). For this reason, SGP-2 has also been designated clusterin (8). As described, the Sertoli cell-secreted SGP-2 or clusterin molecule consists of two monomeric subunits (et and j) which are processed from a propeptide of approximately 64 kilodaltons (kDa).…”

Section: Resultsmentioning

confidence: 99%

Induction of the TRPM-2 gene in cells undergoing programmed death.

Buttyan¹,

Olsson²,

Pintar³

et al. 1989

Mol. Cell. Biol.

449

200

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RNA and protein products encoded by the testosterone-repressed prostate message-2 gene (TRPM-2) are induced to high levels, coordinate with the onset of cell death, in numerous rodent models of inducible tissue damage. These models include cell death initiated by hormonal stimuli (prostate regression), pressure insult (renal atrophy after ureteral obstruction), developmental stimuli (necrosis of interdigital tissue), and cytotoxic injury (chemotherapeutic regression of a tumor). Sequence analysis of cDNA encoding TRPM-2 revealed its close homology with a product referred to as SGP-2 or clusterin expressed constitutively by Sertoli cells; however, the immunologically related polypeptides expressed in regressing tissues differ in molecular mass from the forms secreted by the testis. Although the function(s) of the products encoded by the TRPM-2 gene remains unclear, their presence provides a remarkable and early indicator of programmed cell death in many types of mammalian cells.

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Section: Resultsmentioning

confidence: 99%

Induction of the TRPM-2 gene in cells undergoing programmed death.

Buttyan¹,

Olsson²,

Pintar³

et al. 1989

Mol. Cell. Biol.

449

200

View full text Add to dashboard Cite

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“…The rabbit received yet another booster injection 3 weeks thereafter. Ten days thereafter blood was collected to obtain antiserum (Cheng and Bardin, 1987;Cheng et al, 1988b;Yan and Cheng, 2006), and IgG was isolated by (NH 4 ) 2 SO 4 precipitation and DEAEchromatography by using Macro-PrepH DEAE support (Bio-Rad Laboratories, Hercules, CA) (Cheng et al, 1988a;Page and Thorpe, 2001a;Page and Thorpe, 2001b).…”

Section: Confocal and Electron Microscopymentioning

confidence: 99%

Intercellular adhesion molecule-1 is a regulator of blood–testis barrier function

Xiao

Cheng

Mruk

2012

Journal of Cell Science

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SummaryThe mechanism underlying the movement of preleptotene/leptotene spermatocytes across the blood-testis barrier (BTB) during spermatogenesis is not well understood largely owing to the fact that the BTB, unlike most other blood-tissue barriers, is composed of several co-existing and co-functioning junction types. In the present study, we show that intercellular adhesion molecule-1 [ICAM-1, a Sertoli and germ cell adhesion protein having five immunoglobulin (Ig)-like domains, in addition to transmembrane and cytoplasmic domains] is a regulator of BTB integrity. Initial experiments showed ICAM-1 to co-immunoprecipitate and co-localize with tight junction and basal ectoplasmic specialization proteins such as occludin and N-cadherin, which contribute to BTB function. More importantly, overexpression of ICAM-1 in Sertoli cells in vitro enhanced barrier function when monitored by transepithelial electrical resistance measurements, illustrating that ICAM-1-mediated adhesion can promote BTB integrity. On the other hand, overexpression of a truncated form of ICAM-1 that consisted only of the five Ig-like domains (sICAM-1; this form of ICAM-1 is known to be secreted) elicited an opposite effect when Sertoli cell barrier function was found to be perturbed in vitro; in this case, sICAM-1 overexpression resulted in the downregulation of several BTB constituent proteins, which was probably mediated by Pyk2/p-Pyk2-Y402 and c-Src/pSrc-Y530. These findings were expanded to the in vivo level when BTB function was found to be disrupted following sICAM-1 overexpression. These data illustrate the existence of a unique mechanism in the mammalian testis where ICAM-1 can either positively or negatively regulate BTB function.

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“…Rat clusterin (Cheng et al 1988) and ovine growth hormone (Fleming et al 1997) cDNA probes were verified by restriction analysis. Isolated insert was labelled with [ -32 P]dCTP to specific activities >1 10 8 c.p.m./ µg using random primers (Feinberg & Vogelstein 1983).…”

Section: Gene Probesmentioning

confidence: 99%

Clusterin is expressed in the anterior and intermediate lobes, but not in the posterior pituitary of sheep

Fleming¹,

Hope²,

Bolter³

1999

Journal of Molecular Endocrinology

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We have examined the expression of the ovine clusterin gene in the sheep pituitary gland, with the aim of determining its site of synthesis in this tissue. Northern blotting analysis of extracted polyadenylated RNA, using a 32 P-labelled rat clusterin cDNA probe, detected the greatest amounts of clusterin mRNA in the anterior part of dissected pituitary glands. In situ hybridisation studies showed clusterin mRNA in anterior and intermediate Journal of Molecular Endocrinology (1999) 23, 199-208 INTRODUCTIONClusterin is a highly sulphated glycoprotein that is expressed in a wide range of tissues, often in association with tissue remodelling or apoptosis, in response to injury or pathology, or connected with lipid transport or atherosclerotic vascular disease (Fritz & Murphy 1993). It is expressed in many endocrine tissues, including ovary, testis, prostate and uterus (Sylvester & Griswold 1995), pancreas (Scaglia et al. 1995) and breast tissue (Tenniswood et al. 1992, Welsh 1994. Clusterin is known to be an adrenal chromaffin granule constituent and its expression increases in the adrenal in response to histamine or forskolin treatment (Palmer & Christie 1990, Laslop et al. 1993. In gonadal tissue, large amounts of clusterin mRNA have been measured in extracts of ovine corpora lutea (Fleming et al. 1992) and high concentrations of clusterin protein are synthesised in the ram rete testis (Tung & Fritz 1985).There is further evidence for a role for this protein in search of a function (Fritz 1995) in neural tissue, where its expression is upregulated in pathologies such as Alzheimer's disease (Finch & May 1995). Clusterin is induced in reactive astrocytes in response to neurotoxic injury (Zwain et al. 1994, Walton et al. 1996, Tornquist et al. 1997 and appears to have a protective role in the brain, possibly acting as a local inhibitor of the complement cascade (Tornquist et al. 1996).Clusterin expression is known to be suppressed by gonadal steroids in prostate, mammary gland and uterus (Bettuzzi et al. 1992, Wunsche et al. 1998 and by glucocorticoids in brain and kidney cells (Finch & May 1995, Gutacker et al. 1996. These observations led us to investigate clusterin expression in the ovine pituitary gland, with the aim of determining the distribution of clusterin mRNA and protein in the different parts of this tissue. In previous studies of bovine pituitary, the protein was detected in both the anterior and posterior lobes (Laslop et al. 1993). However, the site of clusterin mRNA transcription remains unclear. Aronow et al. (1993) did not detect clusterin mRNA in mouse anterior pituitary, whereas Laslop et al. (1993) (Fleming et al. 1997) was used as a positive control on Northern blots probed with the growth hormone gene probe.Pituitary glands for immunohistochemistry and in situ hybridisation were obtained from five 4-to 6-year-old Romney ewes killed with Euthatal (Southern Veterinary Supplies, Christchurch, New Zealand; 100 mg/kg, i.v.), at the mid-luteal phase of the oestrous cycle. Whole glands were ...

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Rat clusterin isolated from primary sertoli cell-enriched culture medium is sulfated glycoprotein-2 (SGP-2)

Cited by 89 publications

References 25 publications

Induction of the TRPM-2 gene in cells undergoing programmed death.

Induction of the TRPM-2 gene in cells undergoing programmed death.

Intercellular adhesion molecule-1 is a regulator of blood–testis barrier function

Clusterin is expressed in the anterior and intermediate lobes, but not in the posterior pituitary of sheep

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