Adrenocortical cyclic GMP-dependent protein kinase: Purification, characterization, and modification of its activity by calmodulin, and its relationship with steroidogenesis

Ahrens, Helga; Paul, Aranjaniyil K.; Kuroda, Yoshikazu; Sharma, Rameshwar K.

doi:10.1016/0003-9861(82)90121-7

Cited by 15 publications

(12 citation statements)

References 49 publications

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“…Previous studies have shown that 8-bromo cyclic GMP stimulates steroidogenesis in testicular (Mukhopadhyay et al, 1986b) and isolated fasciculata cells of rat adrenal cortex (Ahrens et al, 1982), and that, in the latter cells, (i) cyclic GMP stimulates cyclic GMP-dependent protein kinase and corticosterone production (Sharma et al, 1976), (ii) cyclic GMP directly stimulates the transformation of cholesterol to corticosterone (Sharma & Sawhney, 1978) and (iii) the steroidogenic potential of Fig. 1.…”

Section: Guanylate Cyclase Activitymentioning

confidence: 95%

“…Abbreviation: DF, dye front. cyclic GMP and its analogues correlates closely with their ability to stimulate cyclic GMP-dependent protein kinase (Ahrens et al, 1982). In addition, cyclic GMPdependent protein kinase has been purified to homogeneity and biochemically characterized in bovine adrenal cortex and isolated rat adrenal cells (Ahrens et al, 1982).…”

Section: Guanylate Cyclase Activitymentioning

confidence: 95%

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Characterization of atrial-natriuretic-factor-receptor-coupled membrane guanylate cyclase from rat and mouse testes

Marala

Sharma

1988

Biochemical Journal

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Studies with isolated adrenal cells and mouse testicular cells have supported a mediatory role of cyclic GMP in ANF (atrial natriuretic factor)-dependent steroidogenic signal transduction. This concept has been strengthened by the purification and biochemical characterization of a 180 kDa protein, which appears to contain both ANF receptor and guanylate cyclase activities, from rat adrenocortical carcinoma cells. Utilizing the antibody to 180 kDa membrane guanylate cyclase as a probe, we now demonstrate the direct presence of ANF-dependent membrane guanylate cyclase in mouse and rat testes. The antibody blocks the ANF-dependent guanylate cyclase activity in isolated membranes, and Western-blot analysis of the partially purified enzyme reveals a single 180 kDa protein. The presence of this enzyme in mouse and rat testes, together with its previous demonstration in rat adrenocortical carcinoma, represent an important potential biochemical role for this enzyme in receptor-mediated steroidogenic signal transduction.

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Section: Guanylate Cyclase Activitymentioning

confidence: 95%

Section: Guanylate Cyclase Activitymentioning

confidence: 95%

Characterization of atrial-natriuretic-factor-receptor-coupled membrane guanylate cyclase from rat and mouse testes

Marala

Sharma

1988

Biochemical Journal

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“…Its important distinctive characteristic that set it apart from the cyclic AMP signaling system was that its most effective effector molecule was 8-bromo cyclic GMP (Ahrens et al, 1982). Compared to its dibutyryl analog, it was 10,000-fold more active in stimulating the protein kinase activity.…”

Section: History: Year 1963–1987mentioning

confidence: 99%

“…Finally, the molecular structure of the cyclic GMP-dependent protein kinase was entirely different from that of the cyclic AMP-dependent protein kinase. The single subunit of the former protein contained both the non-dissociable regulatory and catalytic domains, opposite was the case with the latter protein (Ahrens et al, 1982). Besides providing clarity of the molecular elements of the cyclic GMP signaling system, these unique characteristics of these proteins helped to resolve an earlier argument that cyclic GMP signaling system was the “sub-servant” of the cyclic AMP signaling system (vide supra) .…”

Section: History: Year 1963–1987mentioning

confidence: 99%

Membrane guanylate cyclase, a multimodal transduction machine: history, present, and future directions

Sharma

Duda

2014

Front. Mol. Neurosci.

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A sequel to these authors' earlier comprehensive reviews which covered the field of mammalian membrane guanylate cyclase (MGC) from its origin to the year 2010, this article contains 13 sections. The first is historical and covers MGC from the year 1963–1987, summarizing its colorful developmental stages from its passionate pursuit to its consolidation. The second deals with the establishment of its biochemical identity. MGC becomes the transducer of a hormonal signal and founder of the peptide hormone receptor family, and creates the notion that hormone signal transduction is its sole physiological function. The third defines its expansion. The discovery of ROS-GC subfamily is made and it links ROS-GC with the physiology of phototransduction. Sections ROS-GC, a Ca2+-Modulated Two Component Transduction System to Migration Patterns and Translations of the GCAP Signals Into Production of Cyclic GMP are Different cover its biochemistry and physiology. The noteworthy events are that augmented by GCAPs, ROS-GC proves to be a transducer of the free Ca2+ signals generated within neurons; ROS-GC becomes a two-component transduction system and establishes itself as a source of cyclic GMP, the second messenger of phototransduction. Section ROS-GC1 Gene Linked Retinal Dystrophies demonstrates how this knowledge begins to be translated into the diagnosis and providing the molecular definition of retinal dystrophies. Section Controlled By Low and High Levels of [Ca2+]i, ROS-GC1 is a Bimodal Transduction Switch discusses a striking property of ROS-GC where it becomes a “[Ca2+]i bimodal switch” and transcends its signaling role in other neural processes. In this course, discovery of the first CD-GCAP (Ca2+-dependent guanylate cyclase activator), the S100B protein, is made. It extends the role of the ROS-GC transduction system beyond the phototransduction to the signaling processes in the synapse region between photoreceptor and cone ON-bipolar cells; in section Ca2+-Modulated Neurocalcin δ ROS-GC1 Transduction System Exists in the Inner Plexiform Layer (IPL) of the Retinal Neurons, discovery of another CD-GCAP, NCδ, is made and its linkage with signaling of the inner plexiform layer neurons is established. Section ROS-GC Linkage With Other Than Vision-Linked Neurons discusses linkage of the ROS-GC transduction system with other sensory transduction processes: Pineal gland, Olfaction and Gustation. In the next, section Evolution of a General Ca2+-Interlocked ROS-GC Signal Transduction Concept in Sensory and Sensory-Linked Neurons, a theoretical concept is proposed where “Ca2+-interlocked ROS-GC signal transduction” machinery becomes a common signaling component of the sensory and sensory-linked neurons. Closure to the review is brought by the conclusion and future directions.

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“…The catalytic subunit of cyclic AMP-dependent protein kinase, and the type I and II regulatory subunits of cyclic AMP-dependent protein kinase, from rabbit skeletal muscle and bovine heart, were prepared by the methods of Beavo et al (14) and Dills et al (15), respectively. Cyclic GMP-dependent protein kinase was purified from bovine adrenal cortical tissue as described (16). Protein kinase 380 was purified from bovine adrenal glands according to the procedure of Kuroda and Sharma (17).…”

Section: Methodsmentioning

confidence: 99%

Expression of autophosphorylating protein kinase 500 in normal and neoplastic rat cells.

Majumdar¹,

Cashel²,

Sharma³

1985

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

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Autophosphorylating protein kinase 500 (AUT-PK 500) is a unique serine protein kinase that was originally purified and characterized from the rat adrenocortical carcinoma. A specific RIA with an assay sensitivity of 10 ng (0.02 pmol) was developed for AUT-PK 500 and applied to normal, embryonic, fetal, neonatal, immortal, and neoplastic tissues and cultured cells. As compared to normal rat tissues, the expression of AUT-PK 500 is elevated 100-fold in spontaneously occurring adrenocortical carcinoma 494, 50-to 60-fold in four chemically induced, rapidly growing hepatomas, 30-fold in the chemically induced mammary carcinoma, 20-fold in the cultured hepatoma cell line, and 4-fold in the Rat I and Rat II established tissue culture cell lines. There was also a 5-fold increase in the enzyme when freshly cultured rat skin epitheliallike cells were established. Furthermore, in vivo studies showed that when the rat liver was chemically transformed into its premalignant altered foci, there was a 7-fold elevation of AUT-PK 500. Embryonic cells and fetal and neonatal tissues contained barely detectable (<0.22 ptg/mg of protein) amounts of the protein kinase. These results suggest that AUT-PK 500 is not involved in the differentiation process during fetal development but may be elevated during early steps of carcinogenesis and is further elevated during later stages.

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Adrenocortical cyclic GMP-dependent protein kinase: Purification, characterization, and modification of its activity by calmodulin, and its relationship with steroidogenesis

Cited by 15 publications

References 49 publications

Characterization of atrial-natriuretic-factor-receptor-coupled membrane guanylate cyclase from rat and mouse testes

Characterization of atrial-natriuretic-factor-receptor-coupled membrane guanylate cyclase from rat and mouse testes

Membrane guanylate cyclase, a multimodal transduction machine: history, present, and future directions

Expression of autophosphorylating protein kinase 500 in normal and neoplastic rat cells.

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