Jose Perdomo's research while affiliated with UCSF University of California, San Francisco and other places
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Publications (13)
The molecular weight distribution and Concanavalin A binding properties of labeled glycopeptides and glycoproteins from cell surface membranes, the cytoplasmic fraction and culture media were studied in human fetal and neoplastic colonic cells. Cells were labeled by culturing cells in the presence of [14C]-or[3H]-labeled glucosamine or fucose. Both...
1. A randomly labelled 14C protein was synthesized in order to investigate the site and rate of digestion and absorption of dietary protein in the rat. 2. A liquid test meal consisting of protein and a non-absorbable marker, 51CrCl3, was administered to rats which were then sacrificed at intervals up to 4 hr after ingestion of the meal. Analysis of...
An active multiglycosyltransferase system involved in the transfer of N-acetylgalactosamine, N-acetylglucosamine, and galactose to various glycoprotein acceptors was found in the rat small intestinal mucosa. The present studies are concerned with the subcellular localization of these glycosyltransferases. Satisfactory isolation of smooth and rough...
Optimal assay conditions were determined for four glycosyltransferases in rat small intestinal mucosal homogenates and the regional distribution and cellular localization of these enzymes was studied. For each glycosyltransferase, similar levels of activity were found in duodenal, proximal jejunal and distal ileal segments; activities of the galact...
Membrane glycopeptides were examined in human colonic adenocarcinoma and normal colonic mucosa. The carbohydrates of membrane glycopeptides were found to be markedly reduced in tumor tissue and the relative proportions of the various sugars were altered. Although all of the sugars were lower in tumor tissue when compared to the adjacent normal muco...
The glycoprotein and glycolipid content of brush border and submicrosomal membranes from the mucosa of the rat small intestine was investigated. The microsomal preparations were treated to remove the “non-membranous” material before analysis. In all of the membranes nearly 80% of the carbohydrate was associated with the protein fraction, and 20% wi...
Human serum and hemoglobin-free erythrocyte membranes were found to contain a galactosyltransferase which catalyzes the transfer of galactose from UDP-galactose to specific large and small molecular weight acceptors. The requirements for enzyme activity were found to be similar for the enzymes from both sources. However, the membrane-bound enzyme d...
Serum galactosyltransferase activity was found to be elevated in patients with alcoholic and other liver disorders but remained at a normal level in patients with a variety of nonhepatic diseases. The properties of the galactosyltransferase in patients with liver disease were compared with those of the enzyme in the serum of normal subjects. The po...
Rat small intestinal mucosa was examined for ability to produce mucins with human blood group A, B, and H activity. Blood group activity of the mucins was compared to antigenic activity of red blood cells in individual rats and the enzymatic basis for differences was investigated. Red cells in all the rats examined contained human blood group A and...
A glycosyltransferase, CMP-N-acetylneuraminic acid:glycoprotein sialyltransferase, was found both in human serum and in erythrocycte membranes. The kinetic properties of this enzyme in serum and in erythrocyte membranes were similar although the erythrocyte membrane-bound enzyme required detergents for optimal activity and was unaffected by EDTA, u...
This study demonstrates the presence of an N-acetyl-D-galactosaminyltransferase in human serum and in erythrocyte membranes. This enzyme catalyzes the transfer of N-acetyl-D-galactosamine from UDP-N-acetyl-D-galactosamine to a mucin receptor and 2′-fucosyllactose that have blood group H activity and may be responsible,
therefore, for blood group A...
Citations
... The rationale for this hypothesis is that the intestinal mucosa harbours a heterogeneous population of cells that could be discriminated according to their state of differentiation. Because differentiation of intestinal cells is accompanied by marked changes in the levels of oligo- saccharyltransferases303132333435363738, it is reasonable to assume that the extent of glycosylation of ACE depends on the differentiation state of the various subpopulations of the intestinal cells. To examine this possibility I investigated the biosynthesis of ACE in biopsy specimens taken from patients with CD. ...
![[object Object]](https://i1.rgstatic.net/ii/profile.image/1022740421148673-1620851726387_Q64/Young-Kim-133.jpg)
... It has been reported that neoplastic transformation of the cell is associated with changes in the glycocalyx, in particular with an increased amount of negatively charged glycoproteins (1,7). Increased serum levels of both neutral and acid glycoproteins have been reported since 1944 by Winzler and Burk (15) and then by others, in patients bearing tumors or suffering from nonmalignant diseases such as rheumatoid arthritis, peptic ulcer, and diabetes mellitus (5, 10, 14, :h6). ...
... Total dietary nitrogen (TDN) at each compartment of the GIT tract was calculated as follows: TDN (g) = (TPN − Ep) where Ep is the defined metabolic/endogenous nitrogen. 24,25 Ep refers to nitrogen-containing biomolecules (e.g., proteins and peptides) secreted at each stage of the GIT of an animal receiving a protein-free diet. Ep was calculated for each stage and subtracted to TPN at such stage. ...
... colonic cells frequently reexpress H, A, B, and Le b antigens; therefore, these are considered to be oncofetal tumor-associated antigens (Denk et al., 1975;Cooper et al., 1980;Yonezawa et al., 1982;Brown et al., 1984;Ernst et al., 1984a,b;Yuan et al., 1985;Itzkowitz et al., 1986;Schoentag et al., 1987;Ruggiero et al., 1988;Dabelsteen et al., 1988). Blood group-related antigens are also present in the digestive mucosa of the rat (Kim and Perdomo, 1972;Hansson et al., 1984;Oriol et al., 1986;Decaens et al., 1986), and alterations in their expression have been observed in oral (Reibel et al., 1984(Reibel et al., , 1986 and colonic (Decaens et al., 1986(Decaens et al., , 1988Shioda et al., 1987) mucosae following exposure to chemical carcinogens. However, little is known about the ontogenic expression of BGA in the developing rat colon. ...
... In addition, serum bound sialic acid contents showed no correlation to tissue sialic acid levels in colon cancer [63]. Specifically, studies of Kim and coworkers as well as Dall'Olio et al. reported decreased TSA/ TP content in human colonic tumors compared to the level in normal tissue from the same patients [78][79][80]. ...
Reference: Serum sialylation changes in cancer
... In an early study, Kim and Perdomo (1974) traced the incorporation of [14C]glucosamine into the membranes of intestinal cells. They prepared three membrane fractions, consisting of smooth, rough, and brush border membranes. ...
Reference: Glycosylation in Intestinal Epithelium
... We found that GalNAc-T3 expression was decreased in most tumors, in contrast to its strong expression in normal colorectal mucosa. These data were consistent with previous reports that tumor tissues contained less carbohydrate than normal mucosa, 23,24 with mucins isolated from colon carcinoma showing a reduction of carbohydrate chain number and length compared with mucin from normal mucosa. 25 Vavasseur et al. reported that GalNAc-T3 activity in an intermediate premalignant cell line was twice as high as in an early premalignant cell line, whereas, in a carcinoma cell line, activity was decreased to 61% of that in the early premalignant cell line. ...
... The activation of sialic acid (Neu5Ac) with cytidine monophosphate (CMP) occurs in the nucleus, while all other glycans are activated in the cytosol (Kean et al., 2004) (Nji et al., 2019). The activated nucleotide sugars are transported into the ER and Golgi apparatus by nucleotide sugar transporter (NST) proteins, where they react with the glycosyltransferase enzymes, such as sialyltransferases (STs) or fucosyltransferases (FUTs) to produce a diverse range of glycan structures (Bosmann et al., 1968), (Kim et al., 1971) (van Scherpenzeel et al., 2022). N-Glycan synthesis utilises the lipid carrier dolichol-phosphate (Dol-P) as an oligosaccharide donor (Roth et al., 2010). ...
... Recently, proteolytic release of glycosyltransferase into extracellular space has also been found to regulate cellular activity of glycosyltransferases. Although the presence of cleaved soluble forms of glycosyltransferases in body fluids has been known for a long time [30][31][32][33] , its physiological significance remains elusive. Recently, signal peptide peptidase-like 3 (SPPL3) was identified as being responsible for proteolytic cleavage of various glycosyltransferases [34][35][36] . ...
... Recently, proteolytic release of glycosyltransferase into extracellular space has also been found to regulate cellular activity of glycosyltransferases. Although the presence of cleaved soluble forms of glycosyltransferases in body fluids has been known for a long time [30][31][32][33] , its physiological significance remains elusive. Recently, signal peptide peptidase-like 3 (SPPL3) was identified as being responsible for proteolytic cleavage of various glycosyltransferases [34][35][36] . ...
