Abstract: The subject application provides an aqueous composition suitable for use as an artificial tear solution comprising one or more lipids produced by an enzyme of the diacylglycerol acyltransferase 2 (DGAT2) family and/or the acyl-CoA cholesterol acytransferase (ACAT) family. This invention also provides related methods.

Abstract: This invention provides an isolated nucleic acid which encodes mammalian ACAT-Related Enzyme 2 Required for Viability protein (ARV1p), wherein the encoded ARV1p protein has the amino acid sequence set forth in FIG. 7. This invention provides an isolated nucleic acid which encodes yeast ACAT-Related Enzyme 2 Required for Viability protein (ARV1), wherein the encoded ARV1 protein has the amino acid sequence set forth in FIG. 5. This invention provides a purified mammalian ACAT-Related Enzyme 2 Required for Vialbility protein (ARV1p) having the amino acid sequence set forth in FIG. 7. This invention provides a purified yeast ACAT-Related Enzyme 2 Required for Vialbility protein (ARV1p) having the amino acid sequence set forth in FIG. 5. This invention provides a method for identifying a chemical compound which is capable of inhibiting or stimulating ACAT-Related Enzyme 2 Required for Viability protein (ARV1p) which is capable of inhibiting ARV1p.

Abstract: This invention provides an isolated nucleic acid which encodes mammalian ACAT-Related Enzyme 2 Required for Viability protein (ARV1p), wherein the encoded ARV1p protein has the amino acid sequence set forth in FIG. 7. This invention provides an isolated nucleic acid which encodes yeast ACAT-Related Enzyme 2 Required for Viability protein (ARV1), wherein the encoded ARV1 protein has the amino acid sequence set forth in FIG. 5. This invention provides a purified mammalian ACAT-Related Enzyme 2 Required for Vialbility protein (ARV1p) having the amino acid sequence set forth in FIG. 7. This invention provides a purified yeast ACAT-Related Enzyme 2 Required for Vialbility protein (ARV1p) having the amino acid sequence set forth in FIG. 5. This invention provides a method for identifying a chemical compound which is capable of inhibiting or stimulating ACAT-Related Enzyme 2 Required for Viability protein (ARV1p) which is capable of inhibiting ARV1p.

Abstract: This invention provides an isolated nucleic acid which encodes a diacylglycerol acyltransferase (DGAT); a vector comprising the isolated nucleic acid which encodes a diacylglycerol acyltransferase (DGAT); and a purified poly-peptide which is a diacylglycerol acyltransferase. This invention also provides an in vitro method of detecting a diacylglycerol acyltransferase binding site of an enzyme. This invention provides a method for determining whether a subject known to have an imbalance in trigliceride has the imbalance due to a defect in esterification of diacylglycerol to produce triglyceride. This invention also provides a method for treating a subject who has an imbalance in triglyceride levels due to a defect in esterification of diglycerol which comprises introducing the isolated nucleic acid which encodes a diacylglycerol acyltransferase (DGAT) into the subject under conditions such that the nucleic acid expresses a wildtype diacylglycerol acyltransferase, so as to thereby treat the subject.

Abstract: A truncation of the human LDL receptor gene has been created which can be expressed in a heterologous host to produce a soluble fragment to the receptor protein. The gene can be expressed in insect cells in culture to produce a protein fragment which is not only water soluble but which also retains affinity for binding to LDL. The truncation is a truncation of the carboxyl terminus of the native LDL receptor gene which results in a 354 amino acid protein fragment designated LDL-R.sup.354.

Abstract: A human lipid-associated plasma protein has been produced in vivo in larvae of the Sphingid insect tobacco hornworm, Manduca sexta. The gene for the protein was introduced by recombinant Baculovirus into the body cavity of the larvae, which is a semi-permissive host for the virus. After the larvae had grown further, the hemolymph of the larvae was recovered. The yield of protein produced was much better than could be achieved for the same gene expressed in insect cell culture and a much higher percentage of the protein produced in vivo was associated in lipid particles as compared to the cell culture system. The desired biological activity of the lipid-associated protein was achieved by the in vivo produced protein but not by the protein produced by insect cells in culture.