Induction of type 2 cystatin in rat submandibular glands by systemically administered agents

Cohen, Robert E.; Neiders, Mirdza E.; Bedi, Gurrinder S.; Comeau, Robin L.

doi:10.1016/0003-9969(93)90139-d

Cited by 8 publications

(2 citation statements)

References 30 publications

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“…The common effects of these different noxious stimuli are consistent with a role for rat cystatin S in a response to injury. Consistent with this, SMG acinar cell expression was also found to be induced by the toxic chemicals cyclocytidine (a potent anti-tumor agent with adverse side-effects in humans involving the salivary glands), turpentine (which causes generalized acute inflammation), and potassium dichromate (which causes reversible acute necrosis of renal proximal tubules) (Cohen et al, 1993a). In contrast, another study in SpragueDawley rats found that neither cystatin C nor S is up-regulated…”

Section: (2) Rat Cystatin Smentioning

confidence: 68%

Salivary (SD-Type) Cystatins: Over One Billion Years in the Making—But to What Purpose?

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

103

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The cystatin superfamily is comprised of a large group of ancestrally related proteins, most of which are potent inhibitors of cysteine peptidases (CPs). Human saliva contains relatively abundant proteins that are related ancestrally in sequence to the cystatin superfamily. These proteins are now commonly referred to as 'salivary cystatins', although this is something of a misnomer (see below). It has been several years since the publication of the last comprehensive reviews that focused on the salivary cystatins (Bobek and Levine, 1992;Henskens et al., 1996c). Since then, significant advances have been made regarding the gene organization, protein structure, and properties of human and rat proteins. Therefore, a major purpose of this article is to review this recent work. What is the function of the 'salivary cystatins'? Despite a great deal of research effort, we still do not have a definitive answer to this question. A major impediment is the lack of a disease to associate with a specific defect in a gene: Functionality must be inferred from circumstantial evidence. A central premise of this review is that clues to 'salivary cystatin' function are contained within their phylogenetic history, and that by looking at established or likely functions of their 'siblings' and 'cousins', one can assess the likelihood of this function(s) continuing into the 'salivary cystatins'. A comprehensive review of the large cystatin superfamily is beyond the scope of a single article. This review will aim to outline the main branches of the superfamily and the common elements of their structure and function, but will pay closest attention to the nearest relatives of the 'salivary cystatins'.(1) BACKGROUND Scission of peptide bonds is an essential reaction in living cells, and there is a considerable number of peptidases that catalyze this reaction with various degrees of specificity. CPs use a cysteine residue in the active site as the nucleophile in the reaction (see Dickinson, 2002, and references therein). Release of proteolytic enzymes outside of their normal compartment has the potential to cause serious degradation and pathology-an effect taken advantage of by pathogenic organisms from a wide range of phyla. Therefore, control of proteolytic enzyme activity is mandatory. Building upon a very early report (see Barrett et al., 1986, for a review of this earlier literature) of a bovine trypsin inhibitor in chicken egg white, a search for egg white inhibitors of plant proteinases (the CPs ficin and papain) identified a relatively small (12.7 kDa) protein that was a potent inhibitor (Ki = 10 nM). The term cystatin was coined for this protein, which was shown also to inhibit mammalian CPs of the papain superfamily, including cathepsins B, C, H, and L. Cystatins form 1:1 reversible complexes with CPs, in competition with the substrate, but in some cases the binding is so tight as to be physiologically irreversible. (2) THE CYSTATIN SUPERFAMILYExamination of mammalian tissues and serum revealed several CP inhibitors ranging in si...

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Section: (2) Rat Cystatin Smentioning

confidence: 68%

Salivary (SD-Type) Cystatins: Over One Billion Years in the Making—But to What Purpose?

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

103

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“…Yagil and Barka (1986) induced type 2 cystatin by repeated amputation of continuously erupting mandibular incisor teeth. We have also reported cystatin induction following administration of cyclocytidine, potassium dichromate, and turpentine oil (Cohen et al, 1990b(Cohen et al, , 1993 as well as by the P31-adrenergic agonists dobutamine or methoxyphenamine (Bedi, 1991). We subsequently found that cystatin could be detected immunocytochemically within proximal convoluted tubule cells of kidneys from female rats treated with isoproterenol.…”

Section: Introductionmentioning

confidence: 59%

Induction of Type 2 Salivary Cystatin in Immunological and Chemical Kidney Injury

Cohen

Bedi

Neiders

et al. 1993

Critical Reviews in Oral Biology & Medicine

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We have previously reported that isoproterenol induces type 2 salivary cystatin in both submandibular glands and kidney tubule cells of rats but not in any other organs examined. In the present study, we investigated whether this salivary protein is induced in other conditions that show kidney tubule injury. Immunocytochemistry, using a monospecific antiserum to this cystatin, revealed specific staining within the proximal tubule epithelium of the cortex as well as in the inner and outer stripe of the medulla of immunologically and chemically injured rats. Cystatin could not be detected in kidneys from healthy rats by means of immunocytochemistry. Weak staining was found in 3/3 kidneys of rats treated with turpentine and in 5/5 animals treated with potassium dichromate. In rats treated with puromycin, cystatin could not be demonstrated in 5/5 animals having proteinuria of less than 100 mg/24 h; however, moderate staining was observed in 4/5 puromycin-treated rats having proteinuria greater than 100 mg/24 h. In Heymann nephritis, cystatin was present in 7/31 kidneys with proteinuria lasting 6 to 15 weeks and in none (0/ 7) with proteinuria of shorter duration. Strong staining was also observed in 10/10 kidneys from rats with moderate-to-severe chronic serum sickness. This study shows that elaboration of type 2 cystatin in rats is not limited to salivary glands and, with our previous study, suggests that induction of this cysteine proteinase inhibitor may represent a local response to generalized tissue injury in both submandibular and renal tissues. These findings further demonstrate that induction of cystatin in salivary glands is not unique to these glands and suggest that induction of this cysteine proteinase inhibitor may represent a local response to tissue injury caused by diverse mechanisms.

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Translocation of orally administered rat salivary cystatin into serum and kidney

Nishiura

Ishibashi

Abe

1995

Archives of Oral Biology

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Induction of type 2 cystatin in rat submandibular glands by systemically administered agents

Cited by 8 publications

References 30 publications

Salivary (SD-Type) Cystatins: Over One Billion Years in the Making—But to What Purpose?

Salivary (SD-Type) Cystatins: Over One Billion Years in the Making—But to What Purpose?

Induction of Type 2 Salivary Cystatin in Immunological and Chemical Kidney Injury

Translocation of orally administered rat salivary cystatin into serum and kidney

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