Suraj Bhat | University of California, Los Angeles (original) (raw)
Papers by Suraj Bhat
Page 1. 26 I 5-6 I 04 Developmental Neuroscience Development of the Visual System Guest Editor Su... more Page 1. 26 I 5-6 I 04 Developmental Neuroscience Development of the Visual System Guest Editor Suraf R Bhat, Los Angeles, Calif. SK: n-.-■ Medit-» l iii iL &: iuiil ifiL fMtLldiuri llisel■ Tncihurt Pj. ris-1'l. iHidLm Vv. Vik'll.,:|: I■■-; iiijck.'. it■ S-incnpi^ rf KAKGEK Page 2. ...
Journal of Biological …, Jan 1, 2011
2 The abbreviations used are: ␣B, ␣B-crystallin; DRM, detergent-resistant membrane microdomain; M... more 2 The abbreviations used are: ␣B, ␣B-crystallin; DRM, detergent-resistant membrane microdomain; MBCD, methyl -cyclodextrin; RPE, retinal pigment epithelium; TEM, transmission electron microscopy.
Biochemical and biophysical research …, Jan 1, 1989
... Suraj P. Bhat Corresponding Author Contact Information and Chandrasekharam N. Nagineni. ... 2... more ... Suraj P. Bhat Corresponding Author Contact Information and Chandrasekharam N. Nagineni. ... 2). This may be related to the early functionalmaturation of this tissue (27).ACKNOWLEDGE MENTS: We thank Dr. Joseph Horwitz for providing the antiserum used in thesestudies, Drs. ...
European Journal of …, Jan 1, 1991
Alpha B-crystallin, a polypeptide of molecular mass 22 kDa, is considered to be one of two subuni... more Alpha B-crystallin, a polypeptide of molecular mass 22 kDa, is considered to be one of two subunits (alpha A and alpha B) of the multimeric lens-specific protein, alpha-crystallin. Recent demonstrations of the extra-lenticular presence of alpha B-crystallin have suggested that outside of the lens, this polypeptide may have functions independent of alpha A. Within the lens however, as part of the protein alpha-crystallin, its function is assumed to be structural. In an effort to investigate the functional status of alpha B-crystallin in the lens, we have characterized this polypeptide in the rat heart and the human lens. Unequivocal identity of alpha B-crystallin in the rat heart and the rat lens was established by the sequence analyses of the respective cDNA clones. Size exclusion chromatography (FPLC) and immunoblotting showed that in the rat heart, alpha B-crystallin exists as an aggregate of 300-400 kDa average molecular mass, similar to that of purified alpha B-crystallin isolated from bovine lens. Interestingly, analysis of the human lens proteins by immunoblotting showed that, with age, unlike alpha A-crystallin, the alpha B subunit remains detectable in the soluble fractions derived from normal lenses as old as 82 years. Importantly, the average molecular mass of the alpha B subunit in the soluble fractions prepared from 60-80-year-old human lens nuclei was also found to be 300-400 kDa. These data lead to the conclusion that alpha B-crystallin may exist as an independent protein not only in non-lens tissues (e.g. heart) but in the lens as well.
DNA, Jan 1, 1984
The nucleotide sequence of a cloned cDNA derived from gamma-crystallin mRNA of calf lens was dete... more The nucleotide sequence of a cloned cDNA derived from gamma-crystallin mRNA of calf lens was determined. The cloned cDNA contains the entire coding region 522 bp long, 30 nucleotides of the 5' noncoding region, and 67 residues in the 3' noncoding region followed by a poly(A) tail of 25 nucleotides. The deduced amino acid sequence directly demonstrates for the first time that the calf gamma-crystallin contains 174 residues. The nucleotide sequence contains a number of interesting features including a 32-bp sequence in the 3' region with 70% complementarity to the 3' end of the first monomer unit of the consensus Alu I DNA. Within this region, a 32-bp sequence shows about 80% homology with a segment of hamster 4.5S RNA. The possible evolutionary and regulatory significance of these sequences is discussed.
… Academy of Sciences of the United …, Jan 1, 1979
Bioscience reports, Jan 1, 2001
Experimental eye research, Jan 1, 2004
Journal of Biological Chemistry, Jan 1, 2004
The molecular cascade of stress response in higher eukaryotes commences in the cytoplasm with the... more The molecular cascade of stress response in higher eukaryotes commences in the cytoplasm with the trimerization of the heat shock factor 1 (HSF1), followed by its transport to the nucleus, where it binds to the heat shock element leading to the activation of transcription from the down-stream gene(s). This well-established paradigm has been mostly studied in cultured cells. The developmental and tissue-specific control of the heat shock transcription factors (HSFs) and their interactions with heat shock promoters remain unexplored. We report here that in the rat lens, among the three mammalian HSFs, expression of HSF1 and HSF2 is largely fetal, whereas the expression of HSF4 is predominantly postnatal. Similar pattern of expression of HSF1 and HSF4 is seen in fetal and adult human lenses. This stage-specific inverse relationship between the expression of HSF1/2 and HSF4 suggests tissue-specific management of stress depending on the presence or absence of specific HSF(s). In addition to real-time PCR and immunoblotting, gel mobility shift assays, coupled with specific antibodies and HSE probes, derived from three different heat shock promoters, establish that there is no HSF1 or HSF2 binding activity in the postnatal lens nuclear extracts. Using this unique, developmentally modulated in vivo system, we demonstrate 1) specific patterns of HSF4 binding to heat shock elements derived from alphaB-crystallin, Hsp70, and Hsp82 promoters and 2) that it is HSF4 and not HSF1 or HSF2 that interacts with the canonical heat shock element of the alphaB-crystallin gene.
Journal of Biological Chemistry, Jan 1, 2004
FEBS letters, Jan 1, 1989
Abstract We have recently shown the presence of αB-crystallin in non-ocular tissues of diverse em... more Abstract We have recently shown the presence of αB-crystallin in non-ocular tissues of diverse embryological origins such as the heart, brain, spinal cord, kidney, retina, etc. Using an αB-crystallin-specific antiserum and immunofluorescence, immunoblotting, ...
Page 1. 26 I 5-6 I 04 Developmental Neuroscience Development of the Visual System Guest Editor Su... more Page 1. 26 I 5-6 I 04 Developmental Neuroscience Development of the Visual System Guest Editor Suraf R Bhat, Los Angeles, Calif. SK: n-.-■ Medit-» l iii iL &: iuiil ifiL fMtLldiuri llisel■ Tncihurt Pj. ris-1'l. iHidLm Vv. Vik'll.,:|: I■■-; iiijck.'. it■ S-incnpi^ rf KAKGEK Page 2. ...
Journal of Biological …, Jan 1, 2011
2 The abbreviations used are: ␣B, ␣B-crystallin; DRM, detergent-resistant membrane microdomain; M... more 2 The abbreviations used are: ␣B, ␣B-crystallin; DRM, detergent-resistant membrane microdomain; MBCD, methyl -cyclodextrin; RPE, retinal pigment epithelium; TEM, transmission electron microscopy.
Biochemical and biophysical research …, Jan 1, 1989
... Suraj P. Bhat Corresponding Author Contact Information and Chandrasekharam N. Nagineni. ... 2... more ... Suraj P. Bhat Corresponding Author Contact Information and Chandrasekharam N. Nagineni. ... 2). This may be related to the early functionalmaturation of this tissue (27).ACKNOWLEDGE MENTS: We thank Dr. Joseph Horwitz for providing the antiserum used in thesestudies, Drs. ...
European Journal of …, Jan 1, 1991
Alpha B-crystallin, a polypeptide of molecular mass 22 kDa, is considered to be one of two subuni... more Alpha B-crystallin, a polypeptide of molecular mass 22 kDa, is considered to be one of two subunits (alpha A and alpha B) of the multimeric lens-specific protein, alpha-crystallin. Recent demonstrations of the extra-lenticular presence of alpha B-crystallin have suggested that outside of the lens, this polypeptide may have functions independent of alpha A. Within the lens however, as part of the protein alpha-crystallin, its function is assumed to be structural. In an effort to investigate the functional status of alpha B-crystallin in the lens, we have characterized this polypeptide in the rat heart and the human lens. Unequivocal identity of alpha B-crystallin in the rat heart and the rat lens was established by the sequence analyses of the respective cDNA clones. Size exclusion chromatography (FPLC) and immunoblotting showed that in the rat heart, alpha B-crystallin exists as an aggregate of 300-400 kDa average molecular mass, similar to that of purified alpha B-crystallin isolated from bovine lens. Interestingly, analysis of the human lens proteins by immunoblotting showed that, with age, unlike alpha A-crystallin, the alpha B subunit remains detectable in the soluble fractions derived from normal lenses as old as 82 years. Importantly, the average molecular mass of the alpha B subunit in the soluble fractions prepared from 60-80-year-old human lens nuclei was also found to be 300-400 kDa. These data lead to the conclusion that alpha B-crystallin may exist as an independent protein not only in non-lens tissues (e.g. heart) but in the lens as well.
DNA, Jan 1, 1984
The nucleotide sequence of a cloned cDNA derived from gamma-crystallin mRNA of calf lens was dete... more The nucleotide sequence of a cloned cDNA derived from gamma-crystallin mRNA of calf lens was determined. The cloned cDNA contains the entire coding region 522 bp long, 30 nucleotides of the 5' noncoding region, and 67 residues in the 3' noncoding region followed by a poly(A) tail of 25 nucleotides. The deduced amino acid sequence directly demonstrates for the first time that the calf gamma-crystallin contains 174 residues. The nucleotide sequence contains a number of interesting features including a 32-bp sequence in the 3' region with 70% complementarity to the 3' end of the first monomer unit of the consensus Alu I DNA. Within this region, a 32-bp sequence shows about 80% homology with a segment of hamster 4.5S RNA. The possible evolutionary and regulatory significance of these sequences is discussed.
… Academy of Sciences of the United …, Jan 1, 1979
Bioscience reports, Jan 1, 2001
Experimental eye research, Jan 1, 2004
Journal of Biological Chemistry, Jan 1, 2004
The molecular cascade of stress response in higher eukaryotes commences in the cytoplasm with the... more The molecular cascade of stress response in higher eukaryotes commences in the cytoplasm with the trimerization of the heat shock factor 1 (HSF1), followed by its transport to the nucleus, where it binds to the heat shock element leading to the activation of transcription from the down-stream gene(s). This well-established paradigm has been mostly studied in cultured cells. The developmental and tissue-specific control of the heat shock transcription factors (HSFs) and their interactions with heat shock promoters remain unexplored. We report here that in the rat lens, among the three mammalian HSFs, expression of HSF1 and HSF2 is largely fetal, whereas the expression of HSF4 is predominantly postnatal. Similar pattern of expression of HSF1 and HSF4 is seen in fetal and adult human lenses. This stage-specific inverse relationship between the expression of HSF1/2 and HSF4 suggests tissue-specific management of stress depending on the presence or absence of specific HSF(s). In addition to real-time PCR and immunoblotting, gel mobility shift assays, coupled with specific antibodies and HSE probes, derived from three different heat shock promoters, establish that there is no HSF1 or HSF2 binding activity in the postnatal lens nuclear extracts. Using this unique, developmentally modulated in vivo system, we demonstrate 1) specific patterns of HSF4 binding to heat shock elements derived from alphaB-crystallin, Hsp70, and Hsp82 promoters and 2) that it is HSF4 and not HSF1 or HSF2 that interacts with the canonical heat shock element of the alphaB-crystallin gene.
Journal of Biological Chemistry, Jan 1, 2004
FEBS letters, Jan 1, 1989
Abstract We have recently shown the presence of αB-crystallin in non-ocular tissues of diverse em... more Abstract We have recently shown the presence of αB-crystallin in non-ocular tissues of diverse embryological origins such as the heart, brain, spinal cord, kidney, retina, etc. Using an αB-crystallin-specific antiserum and immunofluorescence, immunoblotting, ...