scholarly journals Gene structure of mouse BIT/SHPS-1

1999 ◽  
Vol 344 (3) ◽  
pp. 667-675 ◽  
Author(s):  
Shin-ichiro SANO ◽  
Hiroshi OHNISHI ◽  
Misae KUBOTA
Keyword(s):  
Amino Acids ◽  
Tyrosine Phosphatase ◽  
Cell Receptor ◽  
Mouse Strains ◽  
Positive Pressure ◽  
Coding Region ◽  
Protein Coding ◽  
Extracellular Region ◽  
The Brain ◽  
Signalling Motifs

BIT/SHPS-1/SIRPα/P84 is a unique molecule with a high degree of homology with immune antigen recognition molecules (immunoglobulin, T-cell receptor and MHC), and is highly expressed in the brain. The extracellular region contains three immunoglobulin-like domains (V-type, C1-type and C1-type), and the intracellular region contains two signalling motifs that interact with SHP-2 protein tyrosine phosphatase. BIT-coated plates support cell-substrate adhesion and neurite extension of neurons, and BIT participates in neuronal signal transduction. Diversity of the V-type domain sequences of human BIT has been reported. In the present study we analysed the structure of the mouse BIT gene (Bit). The protein coding region consists of eight exons corresponding to a signal peptide, a V-type domain, a C1-type domain, a C1-type domain, a transmembrane region and three parts of one cytoplasmic region. The two signalling motifs are encoded in one exon. Four splicing forms of mouse BIT were revealed. We also found the sequence diversity in three mouse strains, namely BALB/c, 129/Sv and C57BL/6. The substitution patterns of amino acids and nucleotides indicate positive pressure to alter the amino acids in the V-type domain in evolution. Immunoblot analyses showed that mouse BIT and human BITα are predominantly expressed in the brain. On the bases of these findings we discuss the possibility that BIT contributes to the genetic individuality and diversity of the brain.

Homology of Glucosyltransferase Gene and Protein Sequences from Streptococcus sobrinus and Streptococcus mutans

1988 ◽  
Vol 67 (3) ◽  
pp. 543-547 ◽  
Author(s):  
R.R.B. Russell ◽  
T. Shiroza ◽  
H.K. Kuramitsu ◽  
J.J. Ferreti
Keyword(s):  
Amino Acids ◽  
Streptococcus Mutans ◽  
Protein Sequences ◽  
Coding Region ◽  
Streptococcus Sobrinus ◽  
Sequence Pattern ◽  
Protein Coding ◽  
High Degree

The sequences of glucosyltransferase genes from Streptococcus sobrinus (gtfI) and Streptococcus mutans (gtfB) were compared and show a high degree of homology. There is a 57.7% homology of nucleotides in the genes and a 56. 7% homology of amino acids in the deduced protein sequences. The G + C content for the protein-coding region is 43.6% for S. sobrinus and 41.2% for S. mutans. Internal repeating sequences present in both proteins exhibit some difference in sequence pattern.

scholarly journals Structure and expression of B-myc, a new member of the myc gene family

1988 ◽  
Vol 8 (8) ◽  
pp. 3168-3174
Author(s):  
S Ingvarsson ◽  
C Asker ◽  
H Axelson ◽  
G Klein ◽  
J Sümegi
Keyword(s):  
Southern Blotting ◽  
Cdna Libraries ◽  
Rat Tissues ◽  
Coding Region ◽  
Specific Expression ◽  
Protein Coding ◽  
Myc Gene ◽  
The Brain ◽  
Mouse Somatic Cell ◽  
Specific Mrna

The myc family of genes contains five functional members. We describe the cloning of a new member of the myc family from rat genomic and cDNA libraries, designated B-myc. A fragment of cloned B-myc was used to map the corresponding rat locus by Southern blotting of DNA prepared from rat X mouse somatic cell hybrids. B-myc mapped to rat chromosome 3. We have previously mapped the c-myc to rat chromosome 7 (J. Sümegi, J. Spira, H. Bazin, J. Szpirer, G. Levan, and G. Klein, Nature [London] 306:497-498, 1983) and N-myc and L-myc to rat chromosomes 6 and 5, respectively (S. Ingvarsson, C. Asker, Z. Wirschubsky, J. Szpirer, G. Levan, G. Klein, and J. Sümegi, Somat. Cell Mol. Genet. 13:335-339, 1987). A partial sequence of B-myc had extensive sequence homology to the c-myc protein-coding region, and the detection of intron homology further indicated that these two genes are closely related. The DNA regions conserved among the myc family members, designated myc boxes, were highly conserved between c-myc and B-myc. A lower degree of homology was detected in other parts of the coding region in c-myc and B-myc not present in N-myc and L-myc. A 1.3-kilobase B-myc-specific mRNA was detected in most rat tissues, with the highest expression in the brain. This resembled the expression pattern of c-myc, although at different relative levels, and was in contrast to the more tissue-specific expression of N-myc and L-myc. B-myc was expressed at uniformly high levels in all fetal tissues and during subsequent postnatal development, in contrast to the stage-specific expression of c-myc.

Cloning and characterization of a cDNA encoding transformation-sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts

1988 ◽  
Vol 8 (1) ◽  
pp. 160-168
Author(s):  
C S Lin ◽  
J Leavitt
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Smooth Muscle ◽  
Rna Splicing ◽  
Human Fibroblasts ◽  
Fibroblast Cell ◽  
Coding Region ◽  
Base Pairs ◽  
Protein Coding ◽  
Peptide Length

We isolated a cDNA clone from the tumorigenic human fibroblast cell line HuT-14 that contains the entire protein coding region of tropomyosin isoform 3 (Tm3) and 781 base pairs of 5'- and 3'-untranslated sequences. Tm3, despite its apparent smaller molecular weight than Tm1 in two-dimensional gels, has the same peptide length as Tm1 (284 amino acids) and shares 83% homology with Tm1. Tm3 cDNA hybridized to an abundant mRNA of 1.3 kilobases in fetal muscle and cardiac muscle, suggesting that Tm3 is related to an alpha fast-tropomyosin. The first 188 amino acids of Tm3 are identical to those of rat or rabbit skeletal muscle alpha-tropomyosin, and the last 71 amino acids differ from those of rat smooth muscle alpha-tropomyosin by only 1 residue. Tm3 therefore appears to be encoded by the same gene that encodes the fast skeletal muscle alpha-tropomyosin and the smooth muscle alpha-tropomyosin via an alternative RNA-splicing mechanism. In contrast to Tm4 and Tm5, Tm3 has a small gene family, with, at best, only one pseudogene.

scholarly journals Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta

Blood ◽  
1994 ◽  
Vol 84 (12) ◽  
pp. 4186-4194 ◽  
Author(s):  
H Honda ◽  
J Inazawa ◽  
J Nishida ◽  
Y Yazaki ◽  
H Hirai
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Chromosomal Localization ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Leukemic Cell ◽  
Coding Region ◽  
Chromosome 11 ◽  
Protein Tyrosine ◽  
Type Iii ◽  
Extracellular Region

Protein-tyrosine phosphatases (PTPases) are considered to play an important role in signal transduction. We previously identified partial sequences of three novel PTPases in a human leukemic cell line. F-36P. We describe here cloning, characterization, and chromosomal localization of one of the newly identified PTPases, termed as HPTP eta (human protein-tyrosine phosphatase eta). The deduced amino acid sequence was composed of an extracellular region homologous to fibronectin type III repeats, a transmembrane region, and a cytoplasmic region containing a single PTPase-like domain. Based on its primary structure, this clone belongs to type-III receptor-type PTPases. The PTPase-like domain showed PTPase activity when expressed in Escherichia coli. Antibody against the extracellular region detected a protein of 220 to 250 kD in human hematopoietic cell lines expressing HPTP eta mRNA. The antibody also recognized a protein of approximately the same molecular weight in COS cells transfected with HPTP eta cDNA, indicating that the antibody specifically recognized HPTP eta gene product and that the cloned cDNA contained full-length coding region. The chromosomal localization determined by fluorescence in situ hybridization showed that the HPTP eta gene was located at chromosome 11p11.2 on the short arm of chromosome 11, which is frequently lost or deleted in human carcinomas.

scholarly journals The complete sequence of the mouse skeletal alpha-actin gene reveals several conserved and inverted repeat sequences outside of the protein-coding region.

1986 ◽  
Vol 6 (1) ◽  
pp. 15-25 ◽  
Author(s):  
M C Hu ◽  
S B Sharp ◽  
N Davidson
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Inverted Repeat ◽  
Actin Gene ◽  
Coding Region ◽  
Specific Expression ◽  
Protein Coding ◽  
Repeat Sequences ◽  
Actin Genes ◽  
Alpha Actin

The complete nucleotide sequence of a genomic clone encoding the mouse skeletal alpha-actin gene has been determined. This single-copy gene codes for a protein identical in primary sequence to the rabbit skeletal alpha-actin. It has a large intron in the 5'-untranslated region 12 nucleotides upstream from the initiator ATG and five small introns in the coding region at codons specifying amino acids 41/42, 150, 204, 267, and 327/328. These intron positions are identical to those for the corresponding genes of chickens and rats. Similar to other skeletal alpha-actin genes, the nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein. Comparison of the nucleotide sequences of rat, mouse, chicken, and human skeletal muscle alpha-actin genes reveals conserved sequences (some not previously noted) outside of the protein-coding region. Furthermore, several inverted repeat sequences, partially within these conserved regions, have been identified. These sequences are not present in the vertebrate cytoskeletal beta-actin genes. The strong conservation of the inverted repeat sequences suggests that they may have a role in the tissue-specific expression of skeletal alpha-actin genes.

scholarly journals CD47 in the Brain and Neurodegeneration: An Update on the Role in Neuroinflammatory Pathways

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3943
Author(s):  
Seyed Mohammad Gheibihayat ◽  
Ricardo Cabezas ◽  
Nikita G. Nikiforov ◽  
Tannaz Jamialahmadi ◽  
Thomas P. Johnston ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Myeloid Leukemia ◽  
Therapeutic Potential ◽  
Lymphoblastic Leukemia ◽  
Tyrosine Phosphatase ◽  
Cell Receptor ◽  
Sh2 Domain ◽  
Ig Superfamily ◽  
The Brain

CD47 is a receptor belonging to the immunoglobulin (Ig) superfamily and broadly expressed on cell membranes. Through interactions with ligands such as SIRPα, TSP-1, integrins, and SH2-domain bearing protein tyrosine phosphatase substrate-1 (SHPS-1), CD47 regulates numerous functions like cell adhesion, proliferation, apoptosis, migration, homeostasis, and the immune system. In this aspect, previous research has shown that CD47 modulates phagocytosis via macrophages, the transmigration of neutrophils, and the activation of T-cells, dendritic cells, and B-cells. Moreover, several studies have reported the increased expression of the CD47 receptor in a variety of diseases, including acute lymphoblastic leukemia (ALL), chronic myeloid leukemia, non-Hodgkin’s lymphoma (NHL), multiple myeloma (MM), bladder cancer, acute myeloid leukemia (AML), Gaucher disease, Multiple Sclerosis and stroke among others. The ubiquitous expression of the CD47 cell receptor on most resident cells of the CNS has previously been established through different methodologies. However, there is little information concerning its precise functions in the development of different neurodegenerative pathologies in the CNS. Consequently, further research pertaining to the specific functions and roles of CD47 and SIRP is required prior to its exploitation as a druggable approach for the targeting of various neurodegenerative diseases that affect the human population. The present review attempts to summarize the role of both CD47 and SIRP and their therapeutic potential in neurodegenerative disorders.

scholarly journals Complete chloroplast genome of Oryza sativa L. (B810s) and its phylogenetic analysis

2021 ◽  
pp. 895-901
Author(s):  
Kebao Song ◽  
Congtian Wang ◽  
Zhongbo Li ◽  
Peng Ning
Keyword(s):  
Amino Acids ◽  
Phylogenetic Analysis ◽  
Oryza Sativa ◽  
Gene Annotation ◽  
Oryza Sativa L ◽  
Amino Acid Sequences ◽  
Coding Region ◽  
Protein Coding ◽  
Cp Genome ◽  
Rna Genes

The complete chloroplast (cp) genome of Oryza sativa L.(B810S) was 134546 bp in length in the study, which contains 149 genes including 99 coding protein genes, 41 transfer RNA genes, 8 ribosomal RNA genes and 1 non-coding region by gene annotation. A total of 20879 amino acids were encoded by this cp genome, TTT (Phe) and TTG (Leu) codon were the most frequent amino acids, whereas the ACC (Thr), GCC (Ala), CTC (Leu), and AAC (Asn) codon were the least frequent ones. The content of the four bases on the cp genome were 30.6% for A, 30.4% for T, 19.4% for C and 19.6% for G, respectively. Obviously, the A+T (61.0%) content is more higher than G+C (39.0%). The gene order and content are the same as those of previously reported cp genome of Rice. Phylogenetic analysis was implemented based on concatenated amino acid sequences of 99 protein-coding genes using Neighbor-Joining method (NJ) method. Therefore, the complete B810S cp genome provides interesting insights and valuable information that can be used to identify related species and reconstruct its phylogeny. Bangladesh J. Bot. 50(3): 895-901, 2021 (September) Special

scholarly journals Structure and expression of B-myc, a new member of the myc gene family.

1988 ◽  
Vol 8 (8) ◽  
pp. 3168-3174 ◽  
Author(s):  
S Ingvarsson ◽  
C Asker ◽  
H Axelson ◽  
G Klein ◽  
J Sümegi
Keyword(s):  
Southern Blotting ◽  
Cdna Libraries ◽  
Rat Tissues ◽  
Coding Region ◽  
Specific Expression ◽  
Protein Coding ◽  
Myc Gene ◽  
The Brain ◽  
Mouse Somatic Cell ◽  
Specific Mrna

The myc family of genes contains five functional members. We describe the cloning of a new member of the myc family from rat genomic and cDNA libraries, designated B-myc. A fragment of cloned B-myc was used to map the corresponding rat locus by Southern blotting of DNA prepared from rat X mouse somatic cell hybrids. B-myc mapped to rat chromosome 3. We have previously mapped the c-myc to rat chromosome 7 (J. Sümegi, J. Spira, H. Bazin, J. Szpirer, G. Levan, and G. Klein, Nature [London] 306:497-498, 1983) and N-myc and L-myc to rat chromosomes 6 and 5, respectively (S. Ingvarsson, C. Asker, Z. Wirschubsky, J. Szpirer, G. Levan, G. Klein, and J. Sümegi, Somat. Cell Mol. Genet. 13:335-339, 1987). A partial sequence of B-myc had extensive sequence homology to the c-myc protein-coding region, and the detection of intron homology further indicated that these two genes are closely related. The DNA regions conserved among the myc family members, designated myc boxes, were highly conserved between c-myc and B-myc. A lower degree of homology was detected in other parts of the coding region in c-myc and B-myc not present in N-myc and L-myc. A 1.3-kilobase B-myc-specific mRNA was detected in most rat tissues, with the highest expression in the brain. This resembled the expression pattern of c-myc, although at different relative levels, and was in contrast to the more tissue-specific expression of N-myc and L-myc. B-myc was expressed at uniformly high levels in all fetal tissues and during subsequent postnatal development, in contrast to the stage-specific expression of c-myc.

scholarly journals Cloning and characterization of a cDNA encoding transformation-sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts.

1988 ◽  
Vol 8 (1) ◽  
pp. 160-168 ◽  
Author(s):  
C S Lin ◽  
J Leavitt
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Smooth Muscle ◽  
Rna Splicing ◽  
Human Fibroblasts ◽  
Fibroblast Cell ◽  
Coding Region ◽  
Base Pairs ◽  
Protein Coding ◽  
Peptide Length

We isolated a cDNA clone from the tumorigenic human fibroblast cell line HuT-14 that contains the entire protein coding region of tropomyosin isoform 3 (Tm3) and 781 base pairs of 5'- and 3'-untranslated sequences. Tm3, despite its apparent smaller molecular weight than Tm1 in two-dimensional gels, has the same peptide length as Tm1 (284 amino acids) and shares 83% homology with Tm1. Tm3 cDNA hybridized to an abundant mRNA of 1.3 kilobases in fetal muscle and cardiac muscle, suggesting that Tm3 is related to an alpha fast-tropomyosin. The first 188 amino acids of Tm3 are identical to those of rat or rabbit skeletal muscle alpha-tropomyosin, and the last 71 amino acids differ from those of rat smooth muscle alpha-tropomyosin by only 1 residue. Tm3 therefore appears to be encoded by the same gene that encodes the fast skeletal muscle alpha-tropomyosin and the smooth muscle alpha-tropomyosin via an alternative RNA-splicing mechanism. In contrast to Tm4 and Tm5, Tm3 has a small gene family, with, at best, only one pseudogene.

scholarly journals The complete sequence of the mouse skeletal alpha-actin gene reveals several conserved and inverted repeat sequences outside of the protein-coding region

1986 ◽  
Vol 6 (1) ◽  
pp. 15-25
Author(s):  
M C Hu ◽  
S B Sharp ◽  
N Davidson
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Inverted Repeat ◽  
Actin Gene ◽  
Coding Region ◽  
Specific Expression ◽  
Protein Coding ◽  
Repeat Sequences ◽  
Actin Genes ◽  
Alpha Actin

The complete nucleotide sequence of a genomic clone encoding the mouse skeletal alpha-actin gene has been determined. This single-copy gene codes for a protein identical in primary sequence to the rabbit skeletal alpha-actin. It has a large intron in the 5'-untranslated region 12 nucleotides upstream from the initiator ATG and five small introns in the coding region at codons specifying amino acids 41/42, 150, 204, 267, and 327/328. These intron positions are identical to those for the corresponding genes of chickens and rats. Similar to other skeletal alpha-actin genes, the nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein. Comparison of the nucleotide sequences of rat, mouse, chicken, and human skeletal muscle alpha-actin genes reveals conserved sequences (some not previously noted) outside of the protein-coding region. Furthermore, several inverted repeat sequences, partially within these conserved regions, have been identified. These sequences are not present in the vertebrate cytoskeletal beta-actin genes. The strong conservation of the inverted repeat sequences suggests that they may have a role in the tissue-specific expression of skeletal alpha-actin genes.

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