Effect of the arginine analog, canavanine, on the synthesis and secretion of procollagen

Schein, Jay; Harsch, Margaret; Cywinski, Anita; Rosenbloom, Joel

doi:10.1016/0003-9861(80)90214-3

Cited by 12 publications

(7 citation statements)

References 23 publications

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“…It seems that amino-acid-analog-containing protein($ are required both for the induction of HSPs and the induced thermal sensitization. The ability of arginine to suppress the canavanine-induced thermal sensitization was not surprising, since it is known that the affinity of the arginyl-tRNA synthetase for arginine is 30-fold higher than for canavanine (Schein et al, 1980). Exponentially growing heat-resistant variants were exposed to 0.6 mM of canavanine in arginine-free medium or 2.5 mM of azetidine in complete medium at 37°C.…”

Section: Discussionmentioning

confidence: 99%

Amino acid analogs while inducing heat shock proteins sensitize CHO cells to thermal damage

Laszlo

1985

Journal Cellular Physiology

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Amino acid analogs have been shown to induce heat shock proteins (HSPs). We have examined the effect of these analogs on the thermal sensitivity of Chinese hamster fibroblasts (HA-1) and their stable heat-resistant variants. We found that exposure of HA-1 cells and their heat-resistant variants to canavanine or L-azetidine-2-carboxylic acid cause enhanced synthesis of the three major mammalian HSPs (molecular weight 70,000, 87,000, and 110,000 kd). Although the synthesis of HSPs was increased, the analogs did not induce thermotolerance, a transient ability to protect cells from thermal damage. On the contrary, the analog treatment increased the thermal sensitivity of HA-1 cells, but not of the heat-resistant strains, when these cells were exposed subsequently to elevated temperatures. Our tentative explanation for these findings is that the incorporation of amino acid analogs into HSPs or other cellular proteins sensitizes HA-1 cells to heat. The heat-resistant strains contain higher levels of constitutive HSPs. The additional functional HSPs in the heat-resistant variants may protect these cells from thermal stress. The presence of some newly synthesized analog-substituted, perhaps nonfunctional, HSPs need not affect this thermal protection.

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Section: Discussionmentioning

confidence: 99%

Amino acid analogs while inducing heat shock proteins sensitize CHO cells to thermal damage

Laszlo

1985

Journal Cellular Physiology

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“…All insects were anesthetized with carbon dioxide before parenteral injection and hemolymph collection. (15,16 7 hr, =7 ml of hemolymph was collected from each group of larvae and treated with phenylthiourea to prevent hemolymph melanization. The hemolymph was centrifuged for 2 min with a Microfuge, and the clarified hemolymph was dialyzed against 500 ml of saline solution (Cherbas';ref.…”

Section: Methodsmentioning

confidence: 99%

“…This arginine analog is activated and aminoacylated by arginyl-tRNA synthetase and then incorporated into nascent polypeptide chains (4,5). Canavanine-containing proteins ("canavanyl proteins") exhibit altered physicochemical properties (6,7); for example, the vitellogenin of Locusta migratoria migratorioides formed in the presence of canavanine possesses an electrophoretic mobility that differs from that of the normal macromolecule (8). Many essential functional properties of proteins synthesized in the presence of canavanine are affected adversely (9).…”

mentioning

confidence: 99%

L-Canavanine and protein synthesis in the tobacco hornworm Manduca sexta.

Rosenthal¹,

Dahlman²

1986

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

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L-Canavanine, a nonprotein amino acid of certain leguminous plants, manifests potent Insecticidal properties in a canavanine-sensitive insect such as the tobacco hornworm Manduca sexta (L.) (Sphingidae). This arginine analog is activated and aminoacylated by arglnyl-tRNA synthetase and incorporated into nascent polypeptide chains to create structurally aberrant, canavanine-containing proteins.Analysis ofincorporation of [3H]leucine into protein inM. sexta larvae that had been injected with canavanine revealed that this arginine analog stimulates protein synthesis. During the first 3 hr after ijection of canavanine, canavanine-mediated net stimulation of protein formation was readily discerned. There. after, the stimulation of protein synthesis appeared to be offset by the preferential degradation of anomalous proteins. Doublelabel protein-turnover experiments with larvae injected with[14C]canavanine-and [3Hlarginine-containing hemolymph proteins showed that canavanine-containing proteins were degraded preferentially.

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“…Studies on chick aorta and copperdeficient pig skin have demonstrated the synthesis of a soluble precursor of elastin (ROSENBLOOM et al 1980). Studies on chick aorta and copperdeficient pig skin have demonstrated the synthesis of a soluble precursor of elastin (ROSENBLOOM et al 1980).…”

Section: Elastinmentioning

confidence: 99%

“…Canavanin is an analogue of arginine which inhibits the normal proteolytic processing of the signal and precursor sequences of the pro collagen molecules and their secretion (SCHEIN et al 1980). …”

Section: Canavaninmentioning

confidence: 99%

Pharmacology of the Skin II

1989

Handbook of Experimental Pharmacology

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PrefaceThe recent interest in the pharmacology of the skin and the treatment of its diseases has come about for two reasons. The first is a realisation that many aspects of pharmacology can be studied as easily in human skin as in animal models, where they may be more relevant to human physiology and disease. Examples of this are the action of various vasoactive agents and the isolation of mediators of inflammation after UV irradiation and antigen-induced dermatitis. The second reason is the fortuitous realisation that a pharmacological approach to the treatment of skin disease need not always await the full elucidation of aetiology and mechanism. For example, whilst the argument continued unresolved as to whether the pilo-sebaceous infection which constitutes acne was due to a blocked duct or to a simple increase in sebum production, 13-cis retinoic acid, was found quite by chance totally to ablate the disease; again, whilst cyclosporin, fresh from its triumphs in organ transplantation, has been found able to suppress the rash of psoriasis, it has resuscitated the debate on aetiology.We are therefore entering a new era in which the pharmacology and clinical pharmacology of skin are being studied as a fascinating new way of exploring questions of human physiology and pharmacology as well as for the development and study of new drugs, use of which will improve disease control and at the same time help to define pathological mechanisms.It was because of this burgeoning interest in pharmacology of skin and its diseases, that this book came about. Indeed it is long overdue and was planned several years ago; we console ourselves with the thought that the delay may have served to help define certain principles which were then only just emerging.The book is divided into two volumes which are independent but complementary; the first being an account of the general pharmacology of skin, the second volume being more concerned with disease and drugs. The first volume is divided into two parts, the one dealing with the pharmacology of skin systems and their control and the other with autocoids in normal and inflamed skin. This second volume has three parts; the first part deals with the methods of measurement which are becoming of increasing importance both in studying the pharmacological effects of drugs and the clinical pharmacology of skin; the second deals with toxicology in its widest sense -including metabolism and percutaneous absorption; and the third is an account both of specific drugs and the drugs used for specific diseases.

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Effect of the arginine analog, canavanine, on the synthesis and secretion of procollagen

Cited by 12 publications

References 23 publications

Amino acid analogs while inducing heat shock proteins sensitize CHO cells to thermal damage

Amino acid analogs while inducing heat shock proteins sensitize CHO cells to thermal damage

L-Canavanine and protein synthesis in the tobacco hornworm Manduca sexta.

Pharmacology of the Skin II

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