Cathepsin Q, a Novel Lysosomal Cysteine Protease Highly Expressed in Placenta

Sol‐Church, Katia; Frenck, Jennifer; Mason, Robert W.

doi:10.1006/bbrc.1999.2051

Cited by 14 publications

(5 citation statements)

References 21 publications

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“…Real time RT-PCR revealed a ubiquitous, mostly low-level expression of cathepsin Q in all mouse tissues except lung where no message was detected (Fig. S8B), which contrasts the prior reported placenta-restricted expression (24). Indeed, the expression of cathepsin Q protein could be detected in bone marrow (Fig.…”

Section: Dna Damage Activates a De Novo Genetic Program To Executecontrasting

confidence: 81%

The p53-cathepsin axis cooperates with ROS to activate programmed necrotic death upon DNA damage

Ren

Wang

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

112

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Three forms of cell death have been described: apoptosis, autophagic cell death, and necrosis. Although genetic and biochemical studies have formulated a detailed blueprint concerning the apoptotic network, necrosis is generally perceived as a passive cellular demise resulted from unmanageable physical damages. Here, we conclude an active de novo genetic program underlying DNA damage-induced necrosis, thus assigning necrotic cell death as a form of ''programmed cell death.'' Cells deficient of the essential mitochondrial apoptotic effectors, BAX and BAK, ultimately succumbed to DNA damage, exhibiting signature necrotic characteristics. Importantly, this genotoxic stress-triggered necrosis was abrogated when either transcription or translation was inhibited. We pinpointed the p53-cathepsin axis as the quintessential framework underlying necrotic cell death. p53 induces cathepsin Q that cooperates with reactive oxygen species (ROS) to execute necrosis. Moreover, we presented the in vivo evidence of p53-activated necrosis in tumor allografts. Current study lays the foundation for future experimental and therapeutic discoveries aimed at ''programmed necrotic death.'' necrosis ͉ BAX ͉ BAK ͉ apoptosis ͉ caspase-independent cell death

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Section: Dna Damage Activates a De Novo Genetic Program To Executecontrasting

confidence: 81%

The p53-cathepsin axis cooperates with ROS to activate programmed necrotic death upon DNA damage

Ren

Wang

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

112

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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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“…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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Cathepsin Q, a Novel Lysosomal Cysteine Protease Highly Expressed in Placenta

Cited by 14 publications

References 21 publications

The p53-cathepsin axis cooperates with ROS to activate programmed necrotic death upon DNA damage

The p53-cathepsin axis cooperates with ROS to activate programmed necrotic death upon DNA damage

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

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

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