S100B‐modulated Ca<sup>2+</sup>‐dependent ROS‐GC1 transduction machinery in the gustatory epithelium: a new mechanism in gustatory transduction

Duda, Teresa; Sharma, Rameshwar K.

doi:10.1016/j.febslet.2004.09.089

Cited by 17 publications

(19 citation statements)

References 48 publications

(94 reference statements)

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“…With the overall goal of determining whether S100B is a natural modulator of ROS-GC1 activity linked with phototransduction in retinal photoreceptors, the presence of S100B protein in the photoreceptor outer segments of mice was assessed by Western blotting using affinity purified S100B antibody [18]. An S100B immunoreactive band was present at the expected molecular weight ( Fig.…”

Section: S100b Is Expressed In Mouse Photoreceptor Outer Segmentsmentioning

confidence: 99%

“…Rabbit S100B and ROS-GC1 antibodies were produced, characterized and affinity purified as in [18,19]. Other antibodies and serum were obtained from commercial sources: goat S100B (N-15) antibody (Santa Cruz Biotechnology, Santa Cruz, CA), rabbit cone arrestin antibody (Millipore, Temecula, CA), rabbit rhodopsin antibody (Abcam, Cambridge, MA), two secondary antibodies, DyLight 649-conjugated donkey anti-goat and DyLight 448-conjugated donkey anti-rabbit, and normal donkey serum (Jackson ImmunoResearch Laboratories, Inc., West Grove, PA).…”

Section: Antibodiesmentioning

confidence: 99%

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S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Wen

Duda²,

Pertzev³

et al. 2012

Cell Physiol Biochem

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Rod outer segment membrane guanylate cyclase (ROS-GC1) is a bimodal Ca²⁺ signal transduction switch. Lowering [Ca²⁺]_i from 200 to 20 nM progressively turns it “ON” as does raising [Ca²⁺]_i from 500 to 5000 nM. The mode operating at lower [Ca²⁺]_i plays a vital role in phototransduction in both rods and cones. The physiological function of the mode operating at elevated [Ca²⁺]_i is not known. Through comprehensive studies on mice involving gene deletions, biochemistry, immunohistochemistry, electroretinograms and single cell recordings, the present study demonstrates that the Ca²⁺-sensor S100B coexists with and is physiologically linked to ROS-GC1 in cones but not in rods. It up-regulates ROS-GC1 activity with a K_1/2 for Ca²⁺ greater than 500 nM and modulates the transmission of neural signals to cone ON-bipolar cells. Furthermore, a possibility is raised that under pathological conditions where [Ca²⁺]_i levels rise to and perhaps even enter the micromolar range, the S100B signaling switch will be turned “ON” causing an explosive production of CNG channel opening and further rise in [Ca²⁺]_i in cone outer segments. The findings define a new cone-specific Ca²⁺-dependent feature of photoreceptors and expand our understanding of the operational principles of phototransduction machinery.

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Section: S100b Is Expressed In Mouse Photoreceptor Outer Segmentsmentioning

confidence: 99%

Section: Antibodiesmentioning

confidence: 99%

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Wen

Duda²,

Pertzev³

et al. 2012

Cell Physiol Biochem

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“…The procedure was carried out according to the previously published protocols (Venkataraman et al, 2000; Duda and Sharma, 2004; Jankowska et al, 2007). 150 mg of membrane fraction proteins were denatured in gel-loading buffer [62.5 mM Tris-HCl (pH 7.5), 2% SDS, 5% glycerol, 1 mM β-mercaptoethanol, and 0.005% bromophenol blue] in 95°C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

“…Beyond the retina, ROS-GC1 is expressed in the pineal gland where in one subset of pinealocytes it co-localizes with GCAP1 and in another, with S100B (Venkataraman et al, 2000); in the mitral cells of the olfactory bulb where it co-localizes with GCAP1 (Duda et al, 2001b); and it co-immunoprecipitates with S100B in the gustatory epithelium (Duda and Sharma, 2004). …”

Section: Introductionmentioning

confidence: 99%

Ca2+-modulated ROS-GC1 transduction system in testes and its presence in the spermatogenic cells

Jankowska

Sharma

Duda

2014

Front. Mol. Neurosci.

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ROS-GC1 belongs to the Ca2+-modulated sub-family of membrane guanylate cyclases. It primarily exists and is linked with signaling of the sensory neurons – sight, smell, taste, and pinealocytes. Exceptionally, it is also present and is Ca2+-modulated in t he non-neuronal cells, the sperm cells in the testes, where S100B protein serves as its Ca2+ sensor. The present report demonstrates the identification of an additional Ca2+ sensor of ROS-GC1 in the testes, neurocalcin δ. Through mouse molecular genetic models, it compares and quantifies the relative input of the S100B and neurocalcin δ in regulating the Ca2+ signaling of ROS-GC1 transduction machinery, and via immunochemistry it demonstrates the co-presence of neurocalcin δ and ROS-GC1 in the spermatogenic cells of the testes. The suggestion is that in more ways than one the Ca2+-modulated ROS-GC1 transduction system is linked with the testicular function. This non-neuronal transduction system may represent an illustration of the ROS-GC1 expanding role in the trans-signaling of the neural and non-neural systems.

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“…The expression of a Ca 2+ signaling ROS-GC1 transduction system in the anterior portion of the bovine gustatory epithelium has been demonstrated at the biochemical, molecular and functional levels (Duda and Sharma, 2004). The system is composed of two components: the Ca 2+ -sensor protein, S100B and the transducer, ROS-GC1.…”

Section: Ros-gc Linkage With Other Than Vision-linked Neuronsmentioning

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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S100B‐modulated Ca²⁺‐dependent ROS‐GC1 transduction machinery in the gustatory epithelium: a new mechanism in gustatory transduction

Cited by 17 publications

References 48 publications

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Ca2+-modulated ROS-GC1 transduction system in testes and its presence in the spermatogenic cells

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

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S100B‐modulated Ca2+‐dependent ROS‐GC1 transduction machinery in the gustatory epithelium: a new mechanism in gustatory transduction

Cited by 17 publications

References 48 publications

S100B Serves as a Ca2+Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

S100B Serves as a Ca2+Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Ca2+-modulated ROS-GC1 transduction system in testes and its presence in the spermatogenic cells

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

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Product

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S100B‐modulated Ca²⁺‐dependent ROS‐GC1 transduction machinery in the gustatory epithelium: a new mechanism in gustatory transduction

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina