Hematologic investigations for 7 years at the Pediatric Department of Yonsei Medical Center of 52 syphilitic infants were reviewed. A moderate degree of anemia with red cell regeneration was observed in 40 infants (76.0%). Marked. thrombocytopenia but without active bleeding was found in 19 infants, and with active bleeding in 3 infants. A wide range of leukocyte counts, relative lymphocytosis and monocytosis were prominant features. The jaundice was mainly due to unconjugated bilirubin in 6 infants, conjugated as well as unconjugated bilirubin in 8 infants. With therapy, the above abnormal hematologic findings showed marked improvement. Early diagnosis is essential. Prevention and congenital syphilis depend on a high level of clinical suspicion, supported by routine and diagnostic use of laboratory and serologic aids, in the asymptomatic or minimally symptomtaic infants.
Bilirubin/blood ; Blood Cell Count ; Blood Platelets ; Female ; Hemoglobins/metabolism ; Human ; Infant, Newborn ; Reticulocytes ; Syphilis, Congenital/blood*

This paper reports an in vivo study on the biophysics characteristics of reticulocytes. Anemia was induced by injection of phenylhydrazine in rabbits. The measurements, including electrophoresis rate, hematolytic rate, fluorescent polarization and the changing anisotropic value, were performed in vivo for 72 hours in the process of reticulocytes growing into erythrocytes. It was shown that there were obvious changes in the biophysics characteristics of reticulocytes in this course. Therefore, the findings are of significance to basic, theoretical and clinical studies.
Anemia, Hemolytic ; blood ; chemically induced ; Animals ; Biophysical Phenomena ; Biophysics ; Erythrocyte Deformability ; Erythrocyte Membrane ; physiology ; Phenylhydrazines ; Rabbits ; Reticulocytes ; metabolism ; physiology

Adult ; Anemia, Iron-Deficiency ; diagnosis ; metabolism ; Female ; Hemoglobins ; analysis ; Humans ; Male ; Middle Aged ; Reference Values ; Reticulocytes ; chemistry ; Young Adult

OBJECTIVETo investigate the difference of the transcripts between reticulocyte and non-reticulocyte cells in human blood.

METHODSGenomic DNA, reticulocyte RNA and total RNA of K-, K+ and Kell-null(K0) were extracted, then PCR, reverse transcription-PCR(RT-PCR) and nested PCR followed by sequencing or cloning-sequencing were used to analyze the KEL gene mRNA exons 1-19 and exons 2-8. Four kinds of monoclonal antibodies were labeled to detect the expression of Kell glycoprotein on red cells or leukocytes with flow cytometry.

RESULTSIn reticulocyte, only one normal KEL transcript faithful to the genomic structure was found in all tested samples except K0 which had 4 different transcripts. Sequence analysis of exons 2-8 of total RNA confirmed the alternative KEL transcripts existed in different samples, mostly caused by abnormal splicing, among them, skipping of exon 3 and a 16 bp insertion of intron 6 at the beginning of exon 7 were the most frequent. Although only one band was observed after amplifying the exons 1-19 from total RNA, the sequencing result showed it was a mixture of different sequences. There was strong expression of Kell glycoprotein on red cells except K0, but no or low expression on leucocytes by flow cytometry.

CONCLUSIONAlternative transcripts of KEL gene exist in different cells, which would be responsible for different Kell glycoprotein expression patterns on different cells. This study suggested that reticulocyte RNA was more suitable than total RNA for molecular study of KEL gene transcription.

Base Sequence ; Cloning, Molecular ; DNA ; genetics ; Exons ; genetics ; Genome, Human ; Genomics ; Humans ; Introns ; genetics ; Kell Blood-Group System ; genetics ; Polymerase Chain Reaction ; RNA, Messenger ; blood ; genetics ; Reticulocytes ; cytology ; metabolism ; Sequence Analysis, DNA

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