Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland.
Annexins are primarily intracellular proteins as would be predicted from their lack of hydrophobic signal sequences. However, we now report that the human prostate gland selectively secretes high concentrations of annexin 1 (also called lipocortin 1 and p35) and a proteolytic cleavage product, des1-29-annexin 1, into seminal plasma. Secreted annexin 1 had a blocked amino terminus and was structurally indistinguishable from intracellular annexin 1. Although annexin 1 and the structurally related protein, annexin 4, co-localized to many of the same cells of the ductal epithelium of the prostate, annexin 4 was not secreted. Thus, the secretion of annexin 1 appears to involve a highly selective mechanism that does not involve targeting to the endoplasmic reticulum by a hydrophobic signal sequence.
Christmas
P
P
Department of Physiology and Biophysics, University of California, Irvine 92717.
Callaway
J
J
Fallon
J
J
Jones
J
J
Haigler
H T
HT
D000595:Amino Acid Sequence; D017302:Annexins; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D005455:Fluorescent Antibody Technique; D006801:Humans; D015151:Immunoblotting; D007124:Immunoenzyme Techniques; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011467:Prostate / Q000378:metabolism*; D021382:Protein Sorting Signals; D012661:Semen / Q000737:chemistry
D017302:Annexins; D002135:Calcium-Binding Proteins; D021382:Protein Sorting Signals