Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2000-04-03
2003-07-08
Achutamurthy, Ponnathapu (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S069100, C435S252300, C435S320100, C536S023200, C424S094640
Reexamination Certificate
active
06589770
ABSTRACT:
BACKGROUND
Proteases are enzymes which digest proteins. Proteases are employed in a variety of applications outside of their natural cellular environment.
For example, in laundry applications proteases are employed as organic catalysts that cause soils to degrade into simpler, more soluble compounds which are then readily removed by water and detergents; i.e., they operate as “stain removers”.
Additionally, it has been reported that certain proteases can provide certain skin conditioning benefits. The stratum corneum is the outermost layer of the epidermis. The cells of the stratum corneum, the corneocytes, represent the end stage of the epidermal differentiation process. Corneocytes are highly resistant anucleated cells mainly consisting of keratin filaments surrounded by a cross-linked protein envelope. A fraction of epidermal cells continuously leave the proliferating basal layer and go through differentiation. Consequently, there is a continuous de novo production of comeocytes. This is balanced to give a constant and well regulated stratum corneum thickness by cell shedding at the skin surface in a process called desquamation. An imbalance between de novo production of the stratum corneum and the rate of desquamation may lead to the formation of scales on the skin surface. Such a condition is commonly seen in diseases such as psoriasis and ichtyosis. The total turnover time of human epidermis is about four to six weeks. Each epidermal cell stays approximately two weeks in the stratum corneum. Desquamation involves elimination of stratum corneum cell cohesion in superficial layers. It must occur in a way that does not interfere with the barrier function of deeper layers, which is dependent on strong intercellular cohesion. It has been reported that proteases may be involved in facilitating desquamation.
Other known uses for proteases include food processing, such as tenderizing meat, producing cheese, and seasoning; fabric processing, such as removing the “scales” from the surface of wool in order to prevent the shrinkage of fabric; and removing the gelatin from the surface of photographic film.
Unfortunately the use of a number of these known proteases is limited by their ability to cause allergic reactions in sensitive individuals, and/or their limited efficacy in various environments. Such allergic reactions can result from actual application of the protease by a sensitive user, such as in applying a skin care product. Alternatively, allergic reactions can occur in individuals intimately involved in the manufacture or packaging of products containing proteases, such as laundry detergents.
Based on the foregoing, there is a need for an alternative protease which is less immunogenic and/or provides superior proteolytic properties. There is also a need for compositions, such as skin care and/or laundry detergent compositions, comprising such a protease.
SUMMARY
The present invention is directed to an isolated polypeptide comprising an amino acid sequence substantially as shown in SEQ ID NO:2, or substantially similar to an amino acid sequence encoded by a nucleotide sequence in a plasmid having all the identifying characteristics of Deposit No. FERM BP-6129.
The present invention is further directed to an isolated polynucleotide comprising a nucleotide sequence substantially as shown in SEQ ID NO:1, or substantially similar to a nucleotide sequence contained in a plasmid having all of the identifying characteristics of Deposit No. FERM BP-6129.
The present invention is further directed to an expression system comprising the above polynucleotide.
The present invention is further directed to a composition comprising the above polypeptide.
The present invention is further directed to a method of treating or preventing skin flaking comprising topical application of a composition comprising the above polypeptide.
The present invention is further directed to an antibody specifically binding the above polypeptide.
These and other features, aspects, and advantages of the present invention will become evident to those skilled in the art from a reading of the present disclosure.
DETAILED DESCRIPTION
While the specification concludes with claims which particularly point out and distinctly claim the invention, it is believed the present invention will be better understood from the following description.
All cited references are incorporated herein by reference in their entireties. Citation of any reference is not an admission regarding any determination as to its availability as prior art to the claimed invention.
All percentages are by weight of total composition unless specifically stated otherwise.
All ratios are weight ratios unless specifically stated otherwise.
Herein, “comprising” means that other steps and other ingredients which do not affect the end result can be added. This term encompasses the terms “consisting of” and “consisting essentially of”.
Herein, “isolated”, in reference to the polypeptide of the present invention or polynucleotide encoding the polypeptide, means that the polypeptide or polynucleotide exists apart from the complex cellular milieu in which it naturally occurs, and the polypeptide is expressible from the polynucleotide in a cell that does not naturally express it when operably linked to the appropriate regulatory sequences. Specifically, when applied to polynucleotides (e.g., DNA), “isolated” indicates the DNA is substantially isolated with respect to (i.e., exists substantially apart from) the complex cellular milieu in which it naturally occurs, or is simply present in a different nucleic acids context from that in which it occurs in nature (for example, when cloned or in the form of a restriction fragment). Thus, the polynucleotide or polypeptide of the invention may be present in a wide variety of vectors, and/or in any of a wide variety of host cells (or other milieu, such as buffers, viruses or cellular extracts), and/or in any variety of compositions; yet still be isolated in the sense used herein in that such vector, host cell or composition is not part of the natural environment of the polynucleotide or polypeptide.
Herein, “KDP” means keratinocyte-derived protease.
Herein, “substantially as shown” or “substantially similar”, with respect to a polynucleotide, means the same or sufficiently similar in structure or nucleotide sequence to encode the desired polypeptide or gene product; or with respect to a polypeptide, the same or sufficiently similar in structure or amino acid sequence to serve its principal function. In other words, a particular subject sequence (amino acid or nucleotide sequence), for example altered by mutagenesis, varies from a reference sequence by one or more substitutions, deletions or additions, the net effect of which is to retain biological activity of the reference polypeptide. Alternatively, nucleotide sequences and analogs are “substantially similar” to the specific nucleotide sequence disclosed herein if the nucleotide sequences, as a result of degeneracy in the genetic code, encode an amino acid sequence substantially similar to the reference amino acid sequence. In addition, “substantially similar” means a polypeptide that will react with antibodies generated against the polypeptide or peptides derived from the polypeptide of the invention.
The present invention relates to newly identified polynucleotides, polypeptides encoded by such polynucleotides, the use of such polynucleotides and polypeptides, the production of such polynucleotides and polypeptides, as well as compositions comprising such polypeptides.
One embodiment of the present invention is contained in DH10B(pBSIISK(+)−KDP1), an
E. coli
strain carrying a plasmid containing DNA encoding a KDP polypeptide. This material has been deposited at the Institute of Bioscience and Human-Technology Agency of Industrial Science and Technology (1-3, Higashi 1 chome Tsukuba-shi Ibaraki-ken 305, Japan) on Sep. 30, 1997. The deposited strain has been assigned Deposit No. FERM BP-6129.
The biological deposit referred to herein will be maintained under
Kitado Haruo
Yoshikawa Akikazu
Zaiki Tomoko
Achutamurthy Ponnathapu
Corstanje Brahm J.
Moore William W.
Paul Andrew A.
The Procter & Gamble & Company
LandOfFree
Keratinocyte derived protease does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Keratinocyte derived protease, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Keratinocyte derived protease will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3005837