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1.
Vet Comp Orthop Traumatol ; 20(3): 219-23, 2007.
Article in English | MEDLINE | ID: mdl-17846689

ABSTRACT

A five-month-old, female Basset Hound was presented for lameness associated with a fused 3rd and 4th digital pad on the left hind limb (simple incomplete syndactyly), and secondary contracture of the deep digital flexure tendon of the 3rd and 4th digit. An onychectomy of the third phalanx of the third and fourth digits was performed. Following the operation, the dog gained good use of the affected limb for one month until intermittent non-weight bearing lameness developed. A second surgery was performed six months later, partially removing the second phalanx of digits three and four. Follow-up reports indicate that the dog is doing well and is without lameness. This is the first report of deep digital flexor tendon contracture and surgical treatment of this complication in canine simple syndactylism.


Subject(s)
Contracture/veterinary , Dog Diseases/diagnosis , Dog Diseases/surgery , Hindlimb/surgery , Syndactyly/veterinary , Tendons/pathology , Animals , Contracture/diagnosis , Contracture/surgery , Diagnosis, Differential , Dog Diseases/diagnostic imaging , Dog Diseases/pathology , Dogs , Female , Hindlimb/abnormalities , Orthopedic Procedures/veterinary , Radiography , Syndactyly/diagnosis , Syndactyly/surgery , Tendons/surgery
2.
EMBO J ; 9(10): 3045-50, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2209537

ABSTRACT

Both genomic and full length cDNA clones of an Arabidopsis thaliana sugar carrier, STP1, have been obtained using a cDNA clone of the H+/hexose cotransporter from the green alga Chlorella kessleri as hybridization probe. The peptide predicted from these sequences in 522 amino acids long and has a molecular weight of 57,518 kd. This higher plant sugar carrier contains 12 putative transmembrane segments and is highly homologous to the H+/hexose cotransporter from Chlorella, with an overall identity in the amino acid sequence of 47.1%. It is also homologous to the human HepG2 glucose transporter (28.4%), and other sugar carriers from man, rat, yeast and Escherichia coli. The definite proof for the function of the STP1 protein as a hexose transporter and data on its substrate specificity were obtained by heterologous expression in the fission yeast Schizosaccharomyces pombe. Transformed yeast cells transport D-glucose with a 100-fold lower KM value than control cells. Moreover only the transformed cells were able to accumulate the non-metabolizable D-glucose analogue 3-O-methyl-D-glucose, indicating that the Arabidopsis carrier catalyses an energy dependent, active uptake of hexoses. Expression of STP1 mRNA is low in heterotrophic tissues like roots or flowers. High levels of expression are found in leaves.


Subject(s)
Arabidopsis Proteins/genetics , Genes, Plant , Monosaccharide Transport Proteins/genetics , Plants/genetics , Amino Acid Sequence , Arabidopsis Proteins/metabolism , Base Sequence , Cloning, Molecular , DNA/genetics , DNA/isolation & purification , Molecular Sequence Data , Monosaccharide Transport Proteins/metabolism , Plants/metabolism , Plasmids , RNA, Messenger/genetics , Recombinant Proteins/metabolism , Restriction Mapping , Schizosaccharomyces/genetics , Sequence Homology, Nucleic Acid , Substrate Specificity
3.
Buenos Aires; Paidós; 4. ed; mayo de 1857. 422 p. (99737).
Monography in Spanish | BINACIS | ID: bin-99737
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