Linked Life Data

10954861

Source:http://linkedlifedata.com/resource/pubmed/id/10954861

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-12-5
pubmed:abstractText
In the present study, we cloned bovine midkine (bMK) cDNA by RT- and RACE-PCR, and determined its nucleotide sequence. The nucleotide and deduced amino acid sequences of bMK showed a high degree of homology to those of mouse and human MK. Moreover, a large amount of recombinant bMK (rbMK) was produced using a baculovirus expression system and the protein was purified to homogeneity by heparin affinity chromatography. To examine whether treatment with rbMK during in vitro maturation (IVM) of bovine cumulus-enclosed oocytes affects their nuclear maturation and postfertilization development to the blastocyst stage, bovine cumulus-enclosed oocytes obtained from slaughterhouse-derived ovaries were cultured for 24 hr in IVM medium without (control) or with various concentrations (50-400 ng/ml) of rbMK, followed by in vitro fertilization (IVF) and culture. Although rbMK treatment during IVM did not affect the rates of nuclear maturation and postfertilization cleavage of oocytes, rbMK at all experimental concentrations significantly (P < 0.05) increased the blastocyst yields per tested and per cleaved oocyte compared to the control. Next, it was examined whether heparitinase (HTN) treatment of cumulus-enclosed oocytes would affect the enhancing activity of rbMK during IVM on the developmental competence of oocyte after IVF. The enhancing activity of rbMK was completely suppressed by HTN (1.0 mU/ml) treatment. These results indicate that the presence of rbMK during IVM of bovine cumulus-enclosed oocytes can enhance their developmental competence to the blastocyst stage after IVF and suggest that heparan sulfate chains on the cell surface of cumulus cells and/or oocytes are required for bMK to exert its effect.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1040-452X
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-107
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10954861-Amino Acid Sequence, pubmed-meshheading:10954861-Amino Acids, pubmed-meshheading:10954861-Animals, pubmed-meshheading:10954861-Base Sequence, pubmed-meshheading:10954861-Carrier Proteins, pubmed-meshheading:10954861-Cattle, pubmed-meshheading:10954861-Cell Line, pubmed-meshheading:10954861-Cloning, Molecular, pubmed-meshheading:10954861-Cytokines, pubmed-meshheading:10954861-DNA, Complementary, pubmed-meshheading:10954861-Female, pubmed-meshheading:10954861-Fertilization, pubmed-meshheading:10954861-Growth Substances, pubmed-meshheading:10954861-Humans, pubmed-meshheading:10954861-Mice, pubmed-meshheading:10954861-Molecular Sequence Data, pubmed-meshheading:10954861-Oocytes, pubmed-meshheading:10954861-Polysaccharide-Lyases, pubmed-meshheading:10954861-Recombinant Fusion Proteins, pubmed-meshheading:10954861-Sequence Analysis, DNA, pubmed-meshheading:10954861-Sequence Homology, Amino Acid, pubmed-meshheading:10954861-Spodoptera
pubmed:year
2000
pubmed:articleTitle
cDNA cloning of bovine midkine and production of the recombinant protein, which affects in vitro maturation of bovine oocytes.
pubmed:affiliation
Laboratory of Reproductive Physiology, Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't