o b j e c t s h a v e m e a n i n g , i f w e a r e o n l y cl ev er en ou gh to d ec ip he r it. T he y ar e st ub bo rn b eca us e th ey s im pl y re fu se to g o aw ay , b y th ei r ve ry p re se nc e de m an di g to b e in te rp re te d. T o hu m an g eo gr ap he rs n o fo rm o f m at er ia l a rt ac t is m or e st ub bo rn , m or e ta nt al iz in g, o r po te ntia lly m or e ilu m in at in...

In Saccharomyces cerevisiae, nascent carboxypeptidase Y (CPY) is directed into the endoplasmic reticulum by an NH2-terminal signal peptide that is removed before the glycosylated protein is transported to the vacuole. In this paper, we show that this signal peptide does not function in mammalian cells: CPY expressed in COS-1 cells is not glycosylated, does not associate with membranes, and reta...

MUC16 is a well-validated cell surface marker for serous adenocarcinomas of the ovary and other gynecologic malignancies that is distinguished by highly repetitive sequences ("mucin repeats") in the extracellular domain (ECD). We produced and compared two monoclonal antibodies: one (11D10) recognizing a unique, nonrepeating epitope in the ECD and another (3A5) that recognizes the repeats and bi...

AIMS To develop a monoclonal antibody specific for human macrophages in routinely processed material. METHODS The monoclonal antibody was derived from a mouse popliteal lymph node after subcutaneous immunisation in the footpad with fragments of human spleen depleted of lymphocytes and erythrocytes. RESULTS 3A5 is a monoclonal antibody reactive with macrophages, monocytes, and histiocytes in...

synthetase-like enzyme. Carboxypeptidase Y (CPY, EC 3.4.16,5) is a yeast vacuolar carboxypeptidase that catalyzes the removal of the C-terminal amino acid from peptides.3) In addition, CPY has aminolytic activity by replacing C-terminal amino acid of the peptide with a free amino acid,4'S) Therefore, CPY seems to participate in the turnover and proteolytic processing of proteins.6) Both hydroly...

CPY is an organophosphorus insecticide that is widely used in North American agriculture. It is non-systemic, comes in several sprayable and granular formulations,and is used on a number of high-acreage crops on which pollinators can forage,including tree fruits, alfalfa, corn, sunflower, and almonds. Bees (Apoidea) are the most important pollinators of agricultural crops in North America and w...

The endoplasmic reticulum (ER) has an elaborate quality control system, which retains misfolded proteins and targets them to ER-associated protein degradation (ERAD). To analyze sorting between ER retention and ER exit to the secretory pathway, we constructed fusion proteins containing both folded carboxypeptidase Y (CPY) and misfolded mutant CPY (CPY*) units. Although the luminal Hsp70 chapero...

In Saccharomyces cerevisiae, transfer of N-linked oligosaccharides is immediately followed by trimming of ER-localized glycosidases. We analyzed the influence of specific oligosaccharide structures for degradation of misfolded carboxypeptidase Y (CPY). By studying the trimming reactions in vivo, we found that removal of the terminal alpha1,2 glucose and the first alpha1,3 glucose by glucosidase...

l hy ll; s K , L ef fle r an d Jo se ph B re nt , Pu bl ic H i s t o r y R e a d i h g s (M al ab ar , e g e r , 1 99 2) ed s, , FL : S A G A O F C O E R ID G E : A S T U D Y I N O R A L H IS T O R Y W ill ia m L yn w oo d M on te ll PR E FA C E C oe R id ge is th e na m e of a ti ny N eg ro c ol on y th at w as n es tle d in th e fo ot hi ls o f th e C um be rl an d M ou nt ai ns in C um be rl...

The folding and assembly of proteins in the endoplasmic reticulum (ER) lumen and membrane are monitored by ER quality control. Misfolded or unassembled proteins are retained in the ER and, if they cannot fold or assemble correctly, ultimately undergo ER-associated degradation (ERAD) mediated by the ubiquitin-proteasome system. Whereas luminal and integral membrane ERAD substrates both require t...