Rat heart fatty acid-binding protein is highly homologous to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin.

Sacchettini, James C.; Said, Boctor; Schulz, Herbert; Gordon, Jeffrey I.

doi:10.1016/s0021-9258(19)83898-x

Cited by 110 publications

(16 citation statements)

References 40 publications

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“…acids reported in the published sequence for rat heart FABP (Sacchettini et al, 1986), although several differences were found. The most striking is at the amino-terminal end, where the first four amino acids predicted by the cDNA sequence (Met-Ala-Asp-Ala) differed completely from the first four amino acids reported by protein sequencing techniques (Thr-Glu-Lys-Asn).…”

Section: Resultsmentioning

confidence: 81%

“…A 24-base oligodeoxynucleotide probe with 32-fold redundancy 1 Abbreviations: FABP, fatty acid binding protein; aa, amino acid; bp, base pair(s); ELISA, enzyme-linked immunosorbent assay; kb, kilobase(s); kDa, kilodalton(s); SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SSC, standard saline-citrate buffer; SSPE, standard saline-sodium phosphate-EDTA buffer; EDTA, ethylenediaminetetraacetic acid. (5'-CTT-CAT-&TA-£TC-SAA-gTT-CTT-3') was synthesized on the basis of amino acids 15-22 of the sequence reported by Sacchettini et al (1986). The two terminal lysine codons were specified as TTC on the basis of codon usage frequencies from isolated eucaryotic cDNAs (Grantham et al, 1981).…”

Section: Methodsmentioning

confidence: 99%

“…Rat heart FABP also has been purified and characterized (Said & Schulz, 1984;Offner et al, 1986) and the complete amino acid sequence determined directly (Sacchettini et al, 1986). Although some homology with the gastrointestinal FABP's was shown, rat heart FABP showed greatest homology to the murine adipocyte "FABP" and to the myelin P2 protein with 62% and 59% homology, respectively (Sacchettini et al, + This work was supported by National Institutes of Health Grants HL 31195 and HL 35700.…”

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confidence: 99%

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Cloning and tissue distribution of rat heart fatty acid binding protein mRNA: identical forms in heart and skeletal muscle

Claffey

Herrera²,

Brecher³

et al. 1987

Biochemistry

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A fatty acid binding protein (FABP) has been identified and characterized in rat heart, but the function and regulation of this protein are unclear. In this study the cDNA for rat heart FABP was cloned from a lambda gt11 library. Sequencing of the cDNA showed an open reading frame coding for a protein with 133 amino acids and a calculated size of 14776 daltons. Several differences were found between the sequence determined from the cDNA and that reported previously by protein sequencing techniques. Northern blot analysis using rat heart FABP cDNA as a probe established the presence of an abundant mRNA in rat heart about 0.85 kilobases in length. This mRNA was detected, but was not abundant, in fetal heart tissue. Tissue distribution studies showed a similar mRNA species in red, but not white, skeletal muscle. In general, the mRNA tissue distribution was similar to that of the protein detected by Western immunoblot analysis, suggesting that heart FABP expression may be regulated at the transcriptional level. S1 nuclease mapping studies confirmed that the mRNA hybridized to rat heart FABP cDNA was identical in heart and red skeletal muscle throughout the entire open reading frame. The structural differences between heart FABP and other members of this multigene family may be related to the functional requirements of oxidative muscle for fatty acids as a fuel source.

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Section: Resultsmentioning

confidence: 81%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Cloning and tissue distribution of rat heart fatty acid binding protein mRNA: identical forms in heart and skeletal muscle

Claffey

Herrera²,

Brecher³

et al. 1987

Biochemistry

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“…Two additional differences were detected at positions 40 and 43, where the MDGI cDNA predicts Thr and Gin instead of Leu and Ser, respectively. The differences might have arisen from genetic polymorphism of the animals, although mutations in the intraspecies variant between binding proteins (FABPs) in heart (15,28,34,44,47), intestine (1, 3), liver (26,54), and mammary gland (8,33,61).…”

Section: Discussionmentioning

confidence: 99%

Developmental regulation of mammary-derived growth inhibitor expression in bovine mammary tissue.

Kurtz

Vogel

Funa

et al. 1990

The Journal of Cell Biology

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Abstract. The cDNA for a previously described growth inhibitor, designated as mammary-derived growth inhibitor (MDGI) (Grosse, R., and P. Langen. 1989. In Handbook of Experimental Pharmacology. In press) has been cloned from a plasmid library which was derived from terminally differentiated bovine mammary gland.Sequencing of the cDNA showed an open reading frame coding for a protein of 133 amino acids. In six positions differences were found between the sequence determined from the cDNA and that determined previously by amino acid sequence analysis. Northern blot analysis revealed abundant MDGI mRNA in the terminally differentiated mammary gland, whereas in virgin gland, liver or pancreas transcripts were not expressed. By use of in situ hybridization technique transcription of MDGI in the developing bovine mammary gland was analyzed.Increasing amounts of MDGI mRNA were detected in the epithelial cells of embryonic mammary rudiment, in the epithelium of developing lobules and in terminal parts of ducts and lobuloalveolar epithelial cells of differentiated glands. There was a geographical gradient of MDGI mRNA concentration in bovine mammary gland reaching a maximum in the proximal parts of the tissue. An immunohistochemical analysis with different polyclonal and peptide directed antibodies against MDGI confirmed the in situ hybridization data with respect to the tissue-specific and differentiation-dependent MDGI expression in bovine mammary gland. The results suggest a close relationship between MDGI transcription and developmental processes in the normal bovine mammary gland.

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“…The amino-acid sequence primary structure of H-FABP has been determined, using protein cleavage techniques, for rat (Sacchettini et al, 1986;Gibson et al, 1988; and human H-FABP (Offner et al, 1988;Börchers et al, 1990), and, making use of nucleotide sequencing, for rat (Claffey et al, 1987;Heuckeroth et al, 1987), cattle (Billich et al, 1988) and mouse H-FABP (Tweedie and Edwards, 1989). These amino acid sequences are shown in Table 2.2.…”

Section: Characteristics Of Heart Type Fatty Acid-binding Protein (H-fabp)mentioning

confidence: 99%

Fatty acid-binding protein in rat heart

Vork¹

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Rat heart fatty acid-binding protein is highly homologous to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin.

Cited by 110 publications

References 40 publications

Cloning and tissue distribution of rat heart fatty acid binding protein mRNA: identical forms in heart and skeletal muscle

Cloning and tissue distribution of rat heart fatty acid binding protein mRNA: identical forms in heart and skeletal muscle

Developmental regulation of mammary-derived growth inhibitor expression in bovine mammary tissue.

Fatty acid-binding protein in rat heart

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