Cloning and Tissue Distribution of a Novel Serine Protease esp-1 from Human Eosinophils

Inoue, Masahiro; Kanbe, Naotomo; Kurosawa, Motohiro; Kido, Hiroshi

doi:10.1006/bbrc.1998.9645

Cited by 36 publications

(26 citation statements)

References 12 publications

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“…By using the pEGFP/TSP50 construct and confocal microscope technique, we found that the TSP50 protein was located in the ER-like structures as well as the cytoplasm membrane. The membrane location was consistent with the fact that TSP50 contains a COOH-terminal hydrophobic membrane-anchoring region, which is also present in a few serine proteases (32)(33)(34). Several reports suggest that these regions could be trans-membrane domains that remain on the membrane after protein shedding (31,35).…”

Section: Discussionsupporting

confidence: 77%

TSP50 Encodes a Testis-Specific Protease and Is Negatively Regulated by p53

Shan

Jurukovski

et al. 2007

Cancer Research

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Earlier studies suggested that TSP50 is a testis-specific gene that encodes a protein, which is homologous to serine proteases but differs in that threonine replaces serine in its catalytic triad. Most importantly, it was abnormally reactivated in many breast cancer biopsies tested. While further investigating its biochemical and cell biological natures, we found that TSP50 exhibited enzyme activity and was located in the endoplasmic reticulum and cytosol membrane. During our studies to elucidate the regulatory mechanisms related to its differential expression, we discovered a putative p53-binding site and several Sp1-binding sites in the TSP50 promoter, which led us to test if it was regulated by the p53 gene. We found that the p53 transgene negatively regulated the TSP50 promoter in diverse types of cell lines. This result was consistent with other observations: (a) p53 overexpression reduced endogenous TSP50 expression; and (b) breast cancer cell lines containing mutated p53, such as MCF7/Adr, or normal p53, such as MCF7, produced high or low levels of TSP50 transcripts, which was consistent with the fact that TSP50 promoter activity was much higher in MCF7/Adr than that in MCF7 cells. We also found that the quantity of Sp1 transcription factor was lower in MCF7/Adr than in MCF7 cells, which suggested that another mechanism (i.e., transcription factor modulation) was also involved in TSP50 differential expression. [Cancer Res 2007;67(3):1239-45]

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Section: Discussionsupporting

confidence: 77%

TSP50 Encodes a Testis-Specific Protease and Is Negatively Regulated by p53

Shan

Jurukovski

et al. 2007

Cancer Research

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“…Testisin belongs to a unique subgroup of trypsin-like serine proteases, which includes prostasin (Yu et al, 1994(Yu et al, , 1995(Yu et al, , 1996, murine and pancreasin (Bhagwandin et al, 2003). These enzymes are synthesised with a distinct carboxy-terminal peptide that is post-transcriptionally modified with a glycosylphosphatidylinositol (GPI)-membrane anchor (Inoue et al, 1998;Hooper et al, 1999;Honda et al, 2002;Netzel-Arnett et al, 2003). Thus, these enzymes may be present in plasma membranes or released from their anchor and secreted.…”

mentioning

confidence: 99%

Hypermethylation of the 5′ CpG island of the gene encoding the serine protease Testisin promotes its loss in testicular tumorigenesis

et al. 2005

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The Testisin gene (PRSS21) encodes a glycosylphosphatidylinositol (GPI)-linked serine protease that exhibits testis tissue-specific expression. Loss of Testisin has been implicated in testicular tumorigenesis, but its role in testis biology and tumorigenesis is not known. Here we have investigated the role of CpG methylation in Testisin gene inactivation and tested the hypothesis that Testisin may act as a tumour suppressor for testicular tumorigenesis. Using sequence analysis of bisulphite-treated genomic DNA, we find a strong relationship between hypermethylation of a 385 bp 5 0 CpG rich island of the Testisin gene, and silencing of the Testisin gene in a range of human tumour cell lines and in 100% (eight/eight) of testicular germ cell tumours. We show that treatment of Testisinnegative cell lines with demethylating agents and/or a histone deacetylase inhibitor results in reactivation of Testisin gene expression, implicating hypermethylation in Testisin gene silencing. Stable expression of Testisin in the Testisin-negative Tera-2 testicular cancer line suppressed tumorigenicity as revealed by inhibition of both anchorage-dependent cell growth and tumour formation in an SCID mouse model of testicular tumorigenesis. Together, these data show that loss of Testisin is caused, at least in part, by DNA hypermethylation and histone deacetylation, and suggest a tumour suppressor role for Testisin in testicular tumorigenesis.

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“…Of these five serine proteases, only Tesp5, which is identical to esp-1 (Inoue et al, 1998), testisin (Scarman et al, 2001), and tryptase 4 (Wong et al, 2001) belonging to a 21st member of serine protease family Prss21, corresponds to the 42-kDa sperm protein (Honda et al, 2002b). Tesp5 is initially synthesized as a 43-kDa precursor in the testis, and the precursor is converted into the 42-and 41-kDa active enzymes during sperm transport in the epididymis.…”

Section: Sperm Penetration Through the Egg Zona Pellucidamentioning

confidence: 99%

Sperm penetration through cumulus mass and zona pellucida

Kim¹,

Yamashita²,

Kimura³

et al. 2008

Int. J. Dev. Biol.

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Mammalian fertilization requires sperm to penetrate the cumulus mass and egg zona pellucida prior to fusion with the egg. Although sperm penetration through these physical barriers is essential, the molecular mechanism has not yet been completely elucidated. In addition to sperm motility, hyaluronan-hydrolyzing and proteolytic enzymes of sperm have been suggested to participate in the penetration events. Here we focus on the functional roles of hyaluronidase and protease in sperm passage through the cumulus mass and zona pellucida.

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Cloning and Tissue Distribution of a Novel Serine Protease esp-1 from Human Eosinophils

Cited by 36 publications

References 12 publications

TSP50 Encodes a Testis-Specific Protease and Is Negatively Regulated by p53

TSP50 Encodes a Testis-Specific Protease and Is Negatively Regulated by p53

Hypermethylation of the 5′ CpG island of the gene encoding the serine protease Testisin promotes its loss in testicular tumorigenesis

Sperm penetration through cumulus mass and zona pellucida

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