Background: A well-informed patient with Type 2 diabetes may be more compliant with treatment. This study aims to evaluate the diabetes-related knowledge and socio demographic determinants of patients seen at University of Santo Tomas Hospital through a translated and validated Filipino-DKT questionnaire.

Methods: Standard translation procedure was used to produce the Filipino version of the DKT2. A convenience sample of 112 outpatients with Type 2 diabetes was identified for six months at the University of Santo Tomas Hospital, Philippines. All data were collected using the Filipino-DKT and a demographic questionnaire.

Results: The Filipino-DKT demonstrated an acceptable Cronbach's alpha of 0.70 and an acceptable average inter-item correlation of 0.40 (p<0.001). The test-retest reliability was excellent, with a Pearson coefficient r of 1.00 (p<0.001). Our study demonstrated that of the 112 patients with diabetes who answered the general knowledge test, the majority had average knowledge of 78.64%, while 16.07% had poor knowledge. A total of 55 participants on insulin answered the second part of Filipino-DKT that measures insulin knowledge. Surprisingly, 56% of the subjects on insulin had poor knowledge, and only 7% had good knowledge. Results showed that the majority (56%) had poor knowledge. Participants who reported poor control of their diabetes (HbA1c >7%) also reported lower levels of knowledge about diabetes and insulin use. There was no association between duration of diabetes, family history of diabetes, and type of diabetes with knowledge of diabetes.

Conclusion: The Filipino diabetic knowledge of diabetes is poor and not related to age, sex, and duration of diabetes. Filipino-DKT is an acceptable, reliable, and valid measure of diabetes knowledge used in our clinical practice and research.

Diabetes Knowledge ; Translation ; Validation

A partial fragment of novel sequence (arr, adriamycin-resistant related) was previously identified using the differential display (DD)-PCR technique with adriamycin-resistant L1210 variant (L1210AdR), which shows a typical multidrug resistant (MDR) phenotypes. The present research shows the isolation of full length arr cDNA sequence. To clone the full length cDNA of arr gene, DD-PCR fragments were subjected to 5'- and 3'-Rapid Amplification of cDNA End (RACE) method. The cloned arr cDNA consisted of 770 bases and contained an open reading frame of 153 bases, encoding a protein of 51 amino acid with the molecular mass of 4 kDa by in vitro translation reactions. Northern blot analysis showed that a 770 bases transcript arr gene was overexpressed in adriamycin-resistant L1210 variant, but not in the parent suggesting that the arr gene may be involved in the adriamycin-resistant phenotypes.
Amino Acid Sequence ; Animal ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA Primers ; Doxorubicin/pharmacology* ; Drug Resistance, Neoplasm/genetics* ; Gene Expression Regulation, Neoplastic ; Glycoproteins/genetics* ; Leukemia L1210/genetics* ; Leukemia L1210/drug therapy ; Mice ; Molecular Sequence Data ; Translation, Genetic

Clathrin-mediated vesicle formation is an essential step in the intracellular trafficking of the protein and lipid. Binding of clathrin assembly protein to clathrin triskelia induces their assembly into clathrin-coated vesicles (CCVs). In order to better understand a possible role of post-translational modification of CALM (clathrin assembly protein lymphoid myeloid), the homologue of AP180, in the assembly of CCVs, CALM was expressed in the cell-free reticulocyte translation system that is capable of carrying out post-translational modification. The apparent molecular weight of the expressed recombinant CALM was estimated as 105 kD. Alkaline phosphatase treatment of CALM resulted in a mobility shift on SDS-PAGE. We found that CALM was associated with the proteins harboring SH3 domain, promote assembly of clathrin triskelia into clathrin cage and bound to the preformed clathrin cage. CALM was also proteolyzed by caspase 3 and calpain but not by caspase 8. These results indicated that the post-translationally modified CALM, expressed in the eukaryotic cell-free reticulocyte translation system was able to mediate the assembly of clathrin and the coated-vesicle formation.
Alkaline Phosphatase/pharmacology ; Animal ; Brain/metabolism ; Calpain/metabolism ; Carrier Proteins/*chemistry ; Caspases/metabolism ; Cattle ; Cell-Free System ; Clathrin/*chemistry ; Electrophoresis, Polyacrylamide Gel ; Glutathione Transferase/metabolism ; Lipids/chemistry ; Membrane Proteins/*chemistry ; Phosphorylation ; Protein Binding ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Protein Transport ; Recombinant Proteins/chemistry/metabolism ; Reticulocytes/metabolism ; Support, Non-U.S. Gov't ; Translation, Genetic ; src Homology Domains