scholarly journals Identification of two cDNA clones encoding small proline-rich proteins expressed in sheep ruminal epithelium

1996 ◽  
Vol 317 (1) ◽  
pp. 225-233 ◽  
Author(s):  
Luquan WANG ◽  
Ransom L. BALDWIN VI ◽  
Barry W. JESSE
Keyword(s):  
Epidermal Keratinocytes ◽  
Cdna Clones ◽  
Type Ii ◽  
Stratum Granulosum ◽  
Specific Expression ◽  
Cornified Envelope ◽  
Human Type ◽  
Epithelial Development ◽  
Ruminal Epithelium

Small proline-rich (SPRR) proteins are markers frequently associated with squamous cell differentiation. They have been proposed to be a novel group of precursor polypeptides for the cornified envelope in epidermal keratinocytes. A plus/minus screening procedure was used to identify cDNA clones expressed in mature but not in neonatal sheep ruminal epithelium. Two clones encoding SPRR proteins were identified and are reported here. Clone 27 encodes an ovine SPRR protein corresponding to the human type-II SPRR protein. Clone 26 encodes an ovine SPRR protein similar to human type-II SPRR protein, but which also contains an N-terminal His-Pro repeat similar to the paired repeats found in the Drosophila paired proteins. The unique combination of a paired domain and an SPRR protein has not been reported prior to this study. The tissue distribution indicates that specific expression of the genes corresponding to these two clones occurs in the epithelium of the ruminant forestomach, and to a lesser extent in skin epithelium. In situ hybridization demonstrated that the SPRR mRNA for both clones were localized in the stratum granulosum, in support of their putative physiological function, i.e. formation of the cornified envelope. Based on Northern blot analysis, mRNA complementary to the two clones appears in the ruminal epithelium by 1 week of age, corresponding to the formation of the stratum granulosum during ruminal epithelial development. The different patterns of changes in amount of mRNA corresponding to these clones during rumen epithelial development indicate that they play different roles in rumen epithelial development.

scholarly journals Tissue-specific expression of the human type II collagen gene in mice.

1987 ◽  
Vol 84 (9) ◽  
pp. 2803-2807 ◽  
Author(s):  
R. H. Lovell-Badge ◽  
A. Bygrave ◽  
A. Bradley ◽  
E. Robertson ◽  
R. Tilly ◽  
...  
Keyword(s):  
Type Ii Collagen ◽  
Collagen Gene ◽  
Type Ii ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Human Type

R-banding and nonisotopic in situ hybridization: precise localization of the human type II collagen gene (COL2A1)

1990 ◽  
Vol 86 (1) ◽  
Author(s):  
Ei-ichi Takahashi ◽  
Tada-aki Hori ◽  
Peter O'Connell ◽  
Mark Leppert ◽  
Ray White
Keyword(s):  
In Situ Hybridization ◽  
Type Ii Collagen ◽  
Collagen Gene ◽  
Type Ii ◽  
Precise Localization ◽  
Human Type

scholarly journals In situ hybridization localizes the human type II alpha 1 collagen gene (COL2A1) to 12q13

Hereditas ◽  
2008 ◽  
Vol 110 (2) ◽  
pp. 165-167 ◽  
Author(s):  
KRISTINA ARHEDEN ◽  
NILS MANDAHL ◽  
SVERRE HEIM ◽  
FELIX MITELMAN
Keyword(s):  
In Situ Hybridization ◽  
Collagen Gene ◽  
Type Ii ◽  
Human Type

Analysis of foetal expression sites of human type II DNA topoisomerase α and β mRNAs by in situ hybridisation

1996 ◽  
Vol 1307 (2) ◽  
pp. 239-247 ◽  
Author(s):  
Dorothea W.J. Zandvliet ◽  
Andrew M. Hanby ◽  
Caroline A. Austin ◽  
Katherine L. Marsh ◽  
Ivan B.N. Clark ◽  
...  
Keyword(s):  
In Situ Hybridisation ◽  
Type Ii ◽  
Dna Topoisomerase ◽  
Human Type

Human type II arginase: sequence analysis and tissue-specific expression

Gene ◽  
1997 ◽  
Vol 193 (2) ◽  
pp. 157-161 ◽  
Author(s):  
Sidney M Morris ◽  
Durga Bhamidipati ◽  
Diane Kepka-Lenhart
Keyword(s):  
Sequence Analysis ◽  
Type Ii ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Human Type

scholarly journals Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry

1991 ◽  
Vol 278 (3) ◽  
pp. 627-635 ◽  
Author(s):  
L A Bobek ◽  
A Aguirre ◽  
M J Levine
Keyword(s):  
Sequence Similarity ◽  
Leader Peptide ◽  
Cdna Clones ◽  
Specific Expression ◽  
Direct Dna Sequencing ◽  
Pcr Products ◽  
Cystatin Gene ◽  
Hybridization In Situ ◽  
Cystatin Sn

A human submandibular-gland (SMG) cDNA library was constructed in a lambda was constructed in a lambda gt11 Sfi-Not orientation-specific expression vector and then screened with antibody generated against human salivary cystatins. The clone C4-4 encoded an N-terminally truncated cystatin S, whereas the others encoded cystatin SN. The library was then rescreened with the C4-4, and the inserts of several positive clones were directly amplified from the eluted plaques by linear PCR and the PCR products analysed by Southern blotting and direct DNA sequencing. Two clones (C3 and C12) encoded a full-length secreted cystatin S and its leader peptide and included 5′- and 3′-untranslated regions. These clones showed a high degree of sequence similarity to cDNA clones encoding human salivary cystatin SN and genomic clones encoding cystatin SN and SA. Hybridization in situ of normal human SMG and parotid-gland (PG) tissue sections localized the cystatin-gene transcripts to the cytoplasm of serous acinar cells of both glands, with a much higher concentration of cystatin mRNA in the SMG. Immunocytochemistry localized the salivary cystatin gene products also to the serous cells, and the levels of cystatin protein correlated with the amount of cystatin mRNA, with a much stronger signal in the SMG than in the PG.

scholarly journals Localization of types I, II, and III collagen mRNAs in developing human skeletal tissues by in situ hybridization

1987 ◽  
Vol 104 (4) ◽  
pp. 1077-1084 ◽  
Author(s):  
M Sandberg ◽  
E Vuorio
Keyword(s):  
In Situ Hybridization ◽  
Type I Collagen ◽  
Cdna Probe ◽  
Type Ii Collagen ◽  
Northern Hybridization ◽  
Cdna Clones ◽  
Sequence Information ◽  
Type I ◽  
Type Ii

Paraffin sections of human skeletal tissues were studied in order to identify cells responsible for production of types I, II, and III collagens by in situ hybridization. Northern hybridization and sequence information were used to select restriction fragments of cDNA clones for the corresponding mRNAs to obtain probes with a minimum of cross-hybridization. The specificity of the probes was proven in hybridizations to sections of developing fingers: osteoblasts and chondrocytes, known to produce only one type of fibrillar collagen each (I and II, respectively) were only recognized by the corresponding cDNA probes. Smooth connective tissues exhibited variable hybridization intensities with types I and III collagen cDNA probes. The technique was used to localize the activity of type II collagen production in the different zones of cartilage during the growth of long bones. Visual inspection and grain counting revealed the highest levels of pro alpha 1(II) collagen mRNAs in chondrocytes of the lower proliferative and upper hypertrophic zones of the growth plate cartilage. This finding was confirmed by Northern blotting of RNAs isolated from epiphyseal (resting) cartilage and from growth zone cartilage. Analysis of the osseochondral junction revealed virtually no overlap between hybridization patterns obtained with probes specific for type I and type II collagen mRNAs. Only a fraction of the chondrocytes in the degenerative zone were recognized by the pro alpha 1(II) collagen cDNA probe, and none by the type I collagen cDNA probe. In the mineralizing zone virtually all cells were recognized by the type I collagen cDNA probe, but only very few scattered cells appeared to contain type II collagen mRNA. These data indicate that in situ hybridization is a valuable tool for identification of connective tissue cells which are actively producing different types of collagens at the various stages of development, differentiation, and growth.

scholarly journals Structure of cDNA clones coding for human type II procollagen. The α 1(II) chain is more similar to the α 1(I) chain than two other α chains of fibrillar collagens

1989 ◽  
Vol 262 (2) ◽  
pp. 521-528 ◽  
Author(s):  
C T Baldwin ◽  
A M Reginato ◽  
C Smith ◽  
S A Jimenez ◽  
D J Prockop
Keyword(s):  
Amino Acid ◽  
Selective Pressure ◽  
Cdna Clones ◽  
Type I ◽  
Type Ii ◽  
Coding Sequences ◽  
Type Iii ◽  
Human Type ◽  
Fibrillar Collagens ◽  
Triple Helical Domain

Overlapping cDNA clones were isolated for human type II procollagen. Nucleotide sequencing of the clones provided over 2.5 kb of new coding sequences for the human pro alpha 1(II) gene and the first complete amino acid sequence of type II procollagen from any species. Comparison with published data for cDNA clones covering the entire lengths of the human type I and type III procollagens made it possible to compare in detail the coding sequences and primary structures of the three most abundant human fibrillar collagens. The results indicated that the marked preference in the third base codons for glycine, proline and alanine previously seen in other fibrillar collagens was maintained in type II procollagen. The domains of the pro alpha 1(II) chain are about the same size as the same domains of the pro alpha chains of type I and type III procollagens. However, the major triple-helical domain is 15 amino acid residues less than the triple-helical domain of type III procollagen. Comparison of hydropathy profiles indicated that the alpha chain domain of type II procollagen is more similar to the alpha chain domain of the pro alpha 1(I) chain than to the pro alpha 2(I) chain or the pro alpha 1(III) chain. The results therefore suggest that selective pressure in the evolution of the pro alpha 1(II) and pro alpha 1(I) genes is more similar than the selective pressure in the evolution of the pro alpha 2(I) and pro alpha 1(III) genes.

Cell-specific expression of fibronectin and EIIIA and EIIIB splice variants after oxygen injury

1998 ◽  
Vol 274 (4) ◽  
pp. L599-L609
Author(s):  
William M. Maniscalco ◽  
Richard H. Watkins ◽  
Patricia R. Chess ◽  
Robert A. Sinkin ◽  
Stuart Horowitz ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Splice Variants ◽  
Large Vessel ◽  
Cell Phenotype ◽  
Type Ii Cells ◽  
Type Ii ◽  
Specific Expression ◽  
Type Ii Cell

Cellular fibronectin (cFN) expression is characteristic of injured tissues. Unlike plasma FN, cFN mRNA often contains the EIIIA or EIIIB domains. We examined the lung cell-specific expression of total cFN mRNA and the EIIIA and EIIIB splice variants in rabbits after acute oxygen injury. By in situ hybridization, control lung had low cFN mRNA. After exposure to >95% oxygen, mRNAs for total cFN and EIIIA were noted primarily in alveolar macrophages and large-vessel endothelial cells. By 3–5 days recovery, cFN and EIIIA mRNA abundance was increased in alveolar septal cells (i.e., alveolar epithelial, interstitial, or endothelial cells) and in some large-vessel endothelial cells but was low in bronchial epithelial cells. During recovery, EIIIB mRNA was low in alveolar septal cells but was noted mainly in chondrocytes. Immunostaining for EIIIA increased during recovery, paralleling the in situ hybridizations. Because FN may modulate alveolar type II cell phenotype, we investigated type II cell cFN mRNA expression in vivo. During recovery, neither isolated type II cells nor cells with surfactant protein C mRNA in vivo contained FN mRNA. In summary, these data suggest that cFN with the EIIIA domain has a role in alveolar cell recovery from oxygen injury and that type II cells do not express cFN during recovery.

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