Appeal No. 1995-2831
Application No. 07/908,376
Vestweber discloses that mitochondria import most of their proteins and small molecules from
the cytoplasm; and, that there is some tentative evidence that they import some of their RNA.
However, it is not known how nucleic acids enter the mitochondria. [Abstract]. Vestweber showed
that at least short pieces of DNA conjugated to a mitochondrial precursor protein can be processed
and transported across the mitochondrial membranes of isolated yeast mitochondria (page 170, col. 2;
page 172, last para.).
Leamon discloses that by conjugating the vitamin folic acid to macromolecules, such as
proteins, enzymes and antisense oligonucleotide, the natural endocytosis pathway for internalizing folate
can also internalize the macromolecules into cultured cells (abstract; page 5572, col. 2; page 5576, col.
1).
Hoflack discloses that phosphomannosyl residues (i.e., phosphorylated (phosphate) mannose
(sugar) residues) on newly synthesized lysosome enzymes (i.e., acid hydrolases) bind to mannose-6-
phosphate receptors in the Golgi which (1) facilitates sorting these lysosomal enzymes from the proteins
which are to be secreted and (2) transports the bound enzymes via coated vesicles to a prelysosomal
acidic compartment where the low pH releases the enzymes. The enzymes are packaged into
lysosomes and the mannose-6-receptors return to the Golgi. Thus, the phosphomannosyl residues on
the acid hydrolase enzymes serve to target these specific enzymes to lysosomes. Hoflack isolated a
second, cation dependent 46 kDa mannose-6-phosphate receptor which is different from the 215 kDa
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