Cloning and expression of a rat placental cDNA encoding a novel cathepsin L‐related protein

Conliffe, Phyllis R.; Ogilvie, Susan; Simmen, Rosalia C. M.; Michel, Frank; Saunders, Paul A.; Shiverick, Kathleen T.

doi:10.1002/mrd.1080400203

Cited by 17 publications

(12 citation statements)

References 40 publications

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“…Sequence similarity and phylogenetic analysis (see Figs. 1, 2) suggest that cathepsin P is the mouse ortholog of a rat placenta-specific CP designated cathepsin Lrelated protein (CLRP) (Conliffe et al, 1995), and cathepsin R (Sol-Church et al, 2000c) is the mouse ortholog of rat cathepsin Q (Sol-Church et al, 2000b). A third distinct mouse placentaspecific CP, designated cathepsin M (Sol-Church et al, 2000a), is closely related to these proteins, although its branch point is less certain (Fig.…”

Section: (E) Cathepsins J P Clrp M Q R and The Testins (I) Propmentioning

confidence: 99%

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

159

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Cysteine peptidases (CPs) are phylogenetically ubiquitous enzymes that can be classified into clans of evolutionarily independent proteins based on the structural organization of the active site. In mammals, two of the major clans represented in the genome are: the CA clan, whose members share a structure and evolutionary history with papain; and the CD clan, which includes the legumains and caspases. This review focuses on the properties of these enzymes, with an emphasis on their potential roles in the oral cavity. The human genome encodes at least (but possibly no more than) 11 distinct enzymes, called cathepsins, that are members of the papain family C1A. Ten of these are present in rodents, which also carry additional genes encoding other cathepsins and cathepsin-like proteins. Human cathepsins are best known from the ubiquitously expressed lysosomal cathepsins B, H, and L, and dipeptidyl peptidase I (DPP I), which until recently were considered to mediate primarily "housekeeping" functions in the cell. However, mutations in DPP I have now been shown to underlie Papillon-Lefèvre syndrome and pre-pubertal periodontitis. Other cathepsins are involved in tissue-specific functions such as bone remodeling, but relatively little is known about the functions of several recently discovered enzymes. Collectively, CPs participate in multiple host systems that are active in health and in disease. They are involved in tissue remodeling and turnover of the extracellular matrix, immune system function, and modulation and alteration of cell function. Intracellularly, CPs function in diverse processes including normal protein turnover, antigen and proprotein processing, and apoptosis. Extracellularly, they can contribute directly to the degradation of foreign proteins and the extracellular matrix. However, CPs can also participate in proteolytic cascades that amplify the degradative capacity, potentially leading to pathological damage, and facilitating the penetration of tissues by cancer cells. We know relatively little regarding the role of human CPs in the oral cavity in health or disease. Most studies to date have focused on the potential use of the lysosomal enzymes as markers for periodontal disease activity. Human saliva contains high levels of cystatins, which are potent CP inhibitors. Although these proteins are presumed to serve a protective function, their in vivo targets are unknown, and it remains to be discovered whether they serve to control any human CP activity.

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Section: (E) Cathepsins J P Clrp M Q R and The Testins (I) Propmentioning

confidence: 99%

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

159

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“…2 [4]). CTSJ shares the highest identity at the amino acid level (85%) with the previously described rat cathepsin L‐related protein (rCLRP [44]) which was deduced from a partial cDNA. This would indicate that CTSJ and rCLRP resemble homologous proteins of different species.…”

Section: Resultsmentioning

confidence: 93%

“…The initiator ATG codon lacks a typical Kozak consensus sequence [43] but three nucleotides 5′ of the initiator codon a characteristic and highly conserved nucleotide A is present. The stop codon is followed by a 199 nucleotide 3′ untranslated region which contains a putative polyadenylation signal (ATTAAA) at position 1254, which parallels the position of the polyadenylation signal of the previously described rat homologue of CTSJ [44]. A poly(A) tract not depicted in Fig.…”

Section: Resultsmentioning

confidence: 98%

Cathepsin J, a novel murine cysteine protease of the papain family with a placenta‐restricted expression

1999

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A novel mouse cysteine protease of the papain family was identified by searching the dbEST database. A 1.28 kb fulllength cDNA was obtained which contains an open reading frame of 999 nucleotides and encodes a predicted polypeptide of 333 amino acids. The deduced polypeptide exhibits features characteristic of cysteine proteases of the papain type including the highly conserved residues of the catalytic triad, and was hence named cathepsin J. Cathepsin J represents the murine homologue of a previously described rat cathepsin L-related protein. Mature cathepsin J shows 59.3% identity to mouse cathepsin L and contains the characteristic ER(F/W)NIN motif within the propeptide indicating that this protease belongs to the subgroup of cathepsin L-like cysteine proteases. Northern blot analysis of various tissues revealed a placenta-restricted expression. This expression pattern may suggest a role of cathepsin J in embryo implantation and/or placental function. Ctsj was mapped to mouse chromosome 13 in the vicinity of cathepsin L suggesting that cathepsin J may have arisen by gene duplication from cathepsin L or a common ancestral gene.z 1999 Federation of European Biochemical Societies.

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“…This cDNA, termed cathepsin L-related protein (CatLRP), was isolated from rat placenta and its sequence was distinct from that of any of the other known proteases [10]. The sequence of CatLRP (accession no.…”

Section: Resultsmentioning

confidence: 99%

Cathepsin P, a novel protease in mouse placenta

Sol‐Church

Frenck

Troeber

et al. 1999

Biochemical Journal

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The complete cDNA nucleotide sequence of a novel cathepsin derived from mouse placenta, termed cathepsin P, was determined. mRNA for cathepsin P was expressed in placenta and at lower levels in visceral yolk sac, but could not be detected in a range of adult tissues. The expression pattern of this protease indicates that it probably plays an important role during implantation and fetal development.

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Cloning and expression of a rat placental cDNA encoding a novel cathepsin L‐related protein

Cited by 17 publications

References 40 publications

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Cathepsin J, a novel murine cysteine protease of the papain family with a placenta‐restricted expression

Cathepsin P, a novel protease in mouse placenta

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