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

Tisljar, Kai; Deussing, Jan M.; Peters, Christoph

doi:10.1016/s0014-5793(99)01263-6

Cited by 17 publications

(13 citation statements)

References 54 publications

(70 reference statements)

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“…2). Cathepsin J/P was shown to map to the same region of mouse chromosome 13 as cathepsin L, consistent with a duplication of a common ancestor of these genes (Tisljar et al, 1999). However, substitutions in the residues located in the S1 and S2 subsites of cathepsin M suggest that these placenta-specific CPs will cleave at different sites.…”

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

confidence: 64%

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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: 64%

“…The mouse CPs designated cathepsin P (Sol-Church et al, 1999a) and cathepsin J (Tisljar et al, 1999) differ by only a single residue insertion, and are most likely the same protein. Sequence similarity and phylogenetic analysis (see Figs.…”

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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“…Another example of functional specialization following duplication of cathepsin genes is provided by the PECs which include cathepsins J, M, Q, R, 3, 6, 7 and 8. They have thus far been found only in rodents, are expressed only in the placenta [64][65][66][67][68][69][70] and several of them are clustered in a multigenic region [71]. On phylogenetic trees, they form a single clade ( Fig.…”

Section: Discussionmentioning

confidence: 99%

Phylogeny of Antigen‐Processing Enzymes: Cathepsins of a Cephalochordate, an Agnathan and a Bony Fish

et al. 2003

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Cathepsins are enzymes that have been cleaving peptide bonds of lysosomal proteins probably since lysosomes appeared in early eucaryotes. When the adaptive system emerged in gnathostomes, cathepsins were recruited to produce peptides for loading onto the major histocompatibility complex class II molecules and for degrading the class II-associated invariant chain just before the loading. The circumstances under which this recruitment took place are unclear because the knowledge about vertebrate cathepsins is limited largely to mammals. To shed light on the recruitment, 10 amphioxus, one lamprey and one cichlid fish cathepsin cDNA clone were characterized and analysed phylogenetically. Disregarding cathepsin O, whose phylogenetic position is uncertain, the analysis confirms the existence of two old lines of descent, the B and the L lineages of cathepsins, which diverged from each other early in the evolution of eucaryotes. The B lineage encompasses cathepsins B, C and Z (X). The L lineage splits off sublineages encompassing cathepsins F and W before the plant-animal separation and cathepsin H early in the evolution of the metazoa. The remaining cathepsins belonging to the L lineage diverged from one another during the evolution of vertebrates: S, K and L before the emergence of bony fishes, and the group of rodent placentally expressed cathepsins [J (P), M, Q, R, 3, 6, 7 and 8] as well as the testis/ova-expressed cathepsins (testins) probably after the divergence of rodents from primates. The part possibly played by the adaptive immune system in some of these divergences is discussed.

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“…They are involved in diverse biological functions including bulk protein turnover [14,15], protein processing [16], antigen presentation [17], chronic inflammation [18], bone resorption [19] and tumour formation and metastasis [20,21]. Tissue distribution of each member of this family differs considerably from the others [22]. Some members including cathepsin B, H and L are expressed ubiquitously whereas others such as cathepsin K, S and W are expressed only in restricted tissues and are possibly involved in some specific functions.…”

Section: Discussionmentioning

confidence: 99%

Cathepsin Gene Expression in Mouse Placenta during the Latter Half of Pregnancy

Ishida

Ono

Taguchi

et al. 2004

Journal of Reproduction and Development

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Abstract. Gene expressions and their interaction are complex and have not been definitely clarified in the placenta. To identify interactions of gene products previously not studied, we applied cDNA subtraction analyses to the placenta between days 12 and 16, days 12 and 14, days 14 and 16 of pregnancy. Among subtracted cDNAs cathepsin M, Q and R in PECs were specifically identified on days 14 and 16 pregnancy. All of these gene expressions exhibited a similar pattern to the mPL-II gene expression determined by northern blot and RT-PCR analyses. By means of in situ hybridization, these mRNAs were localized in the basal and labyrinth zones of the placenta on day 16 of pregnancy. Double staining studies of cathepsin Q or cathepsin R mRNA by in situ hybridization followed by immunohistochemical staining of mPL-II in the same section revealed that signals for cathepsin Q and cathepsin R mRNAs were colocalized in mPL-II immunopositive trophoblast cells in the basal and labyrinth zones of the placenta on day 16 of pregnancy. Possible association of cathepsins with mPL-II may play important roles in placental functions during the latter half of pregnancy in mice.

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

Cited by 17 publications

References 54 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

Phylogeny of Antigen‐Processing Enzymes: Cathepsins of a Cephalochordate, an Agnathan and a Bony Fish

Cathepsin Gene Expression in Mouse Placenta during the Latter Half of Pregnancy

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