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Stanford researchers find hair growth trigger


#1

Something to do with a molecule called laminin-511, and Dr. Cotsarelis chimes-in in the article. Unfortunately, it’s research merely at the mouse stage right now.


By Vianna Davila
Mercury News
Article Launched: 07/31/2008 02:19:52 PM PDT

Watch out, Rogaine.
Stanford University researchers have pinpointed a molecule that triggers hair follicle growth in mice, a treatment that one day could eventually mean some shaggy dos, or at least a few more strands, for humans who have experienced hair loss.

The report, published today in the Journal of Genes and Development, focuses on a molecule called laminin-511. The molecule acts like an operator, transferring messages, or proteins, between the outer and inner layers of skin, an exchange that ultimately drives hair formation.

Unlike Rogaine or Propecia, products that slow hair loss, researchers hope the laminin-511 could potentially regenerate the actual follicles that grow hair.

“Loss of hair is not going to kill anybody,” said Dr. Peter Marinkovich, the study’s senior author and an associate professor at Stanford University’s School of Medicine. “At the same time, for some people, hair loss can be a really traumatic thing, especially for women.”

He hopes the treatment eventually could help patients who suffer from alopecia, a disorder that can cause hair loss in patches, or speed up hair growth for chemotherapy patients.

Evidence suggests laminin-511 could lead to more than fuller heads of hair: researchers believe the molecule might have the ability to regenerate other developing tissues, like limbs or even organs; but further tests are necessary to understand exactly how that process works.

In an earlier study using mice,

Stanford researchers showed laminin-511 was essential for hair growth but they were unsure why. The recent study more clearly demonstrated how the molecule transfers signals within the skin in a way that particularly stimulates follicle growth. How soon did scientists see results? Mice injected with the purified molecule grew back hair in two weeks, at half the thickness of a normal rodent.
But if you’re itching for a dose of laminin-511 to restore your once long locks, hold off on buying that bottle of hair gel - Do-It-Yourself treatments are likely years away.

The Stanford study presents a new understanding of how laminin-511 works, said Dr. George Cotsarelis, director of the Hair and Scalp Clinic at the University of Pennsylvania School of Medicine. But more clinical trials are necessary to show how humans will react to the treatment.

Marinkovich said his team hopes to repeat the tests on animals treated with chemotherapy and later on human subjects.

The findings are “important in the long run,” Cotsarelis said, calling the Stanford study, “one of the initial steps.”

Contact Vianna Davila at vdavila at mercurynews dot com or (408) 920-5064.

.


#2

I can’t open the link


#3

» I can’t open the link

I just added the article in my original post.


#4

» » I can’t open the link
»
» I just added the article in my original post.

thank you, however, nothing useful for us… :frowning:


#5

» » » I can’t open the link
» »
» » I just added the article in my original post.
»
» thank you, however, nothing useful for us… :frowning:

The Laminin 511/521–binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3
Tosti J. Mankelow1, Nicholas Burton2, Fanney O. Stefansdottir1, Frances A. Spring1, Stephen F. Parsons1, Jan S. Pedersen3, Cristiano L. P. Oliveira3, Donna Lammie4, Timothy Wess4, Narla Mohandas5, Joel Anne Chasis6, R. Leo Brady2, and David J. Anstee1

1 Bristol Institute for Transfusion Sciences (BITS), National Blood Service, Bristol, United Kingdom; 2 Department of Biochemistry, University of Bristol, Bristol, United Kingdom; 3 Department of Chemistry, University of Aarhus, Aarhus, Denmark; 4 School of Optometry and Vision Sciences, Cardiff University, Cardiff, United Kingdom; 5 New York Blood Center, New York City; and 6 University of California, Lawrence Berkeley National Laboratory, Berkeley

The Lutheran blood group glycoprotein, first discovered on erythrocytes, is widely expressed in human tissues. It is a ligand for the {alpha}5 subunit of Laminin 511/521, an extracellular matrix protein. This interaction may contribute to vaso-occlusive events that are an important cause of morbidity in sickle cell disease. Using x-ray crystallography, small-angle x-ray scattering, and site-directed mutagenesis, we show that the extracellular region of Lutheran forms an extended structure with a distinctive bend between the second and third immunoglobulin-like domains. The linker between domains 2 and 3 appears to be flexible and is a critical determinant in maintaining an overall conformation for Lutheran that is capable of binding to Laminin. Mutagenesis studies indicate that Asp312 of Lutheran and the surrounding cluster of negatively charged residues in this linker region form the Laminin-binding site. Unusually, receptor binding is therefore not a function of the domains expected to be furthermost from the plasma membrane. These studies imply that structural flexibility of Lutheran may be essential for its interaction with Laminin and present a novel opportunity for the development of therapeutics for sickle cell disease.

correct me if I am wrong, but is not Acell simply an extracellular matrix? if so it should contain this protein. what does this mean in regards to how Acell effects our hair follicles, I have no idea but hopefully it could help our struggle.


#6

» The Laminin 511/521–binding site on the Lutheran blood group glycoprotein
» is located at the flexible junction of Ig domains 2 and 3
» Tosti J. Mankelow1, Nicholas Burton2, Fanney O. Stefansdottir1, Frances A.
» Spring1, Stephen F. Parsons1, Jan S. Pedersen3, Cristiano L. P. Oliveira3,
» Donna Lammie4, Timothy Wess4, Narla Mohandas5, Joel Anne Chasis6, R. Leo
» Brady2, and David J. Anstee1
»
» 1 Bristol Institute for Transfusion Sciences (BITS), National Blood
» Service, Bristol, United Kingdom; 2 Department of Biochemistry, University
» of Bristol, Bristol, United Kingdom; 3 Department of Chemistry, University
» of Aarhus, Aarhus, Denmark; 4 School of Optometry and Vision Sciences,
» Cardiff University, Cardiff, United Kingdom; 5 New York Blood Center, New
» York City; and 6 University of California, Lawrence Berkeley National
» Laboratory, Berkeley
»
» The Lutheran blood group glycoprotein, first discovered on erythrocytes,
» is widely expressed in human tissues. It is a ligand for the {alpha}5
» subunit of Laminin 511/521, an extracellular matrix
» protein. This interaction may contribute to vaso-occlusive
» events that are an important cause of morbidity in sickle cell disease.
» Using x-ray crystallography, small-angle x-ray scattering, and
» site-directed mutagenesis, we show that the extracellular region of
» Lutheran forms an extended structure with a distinctive bend between the
» second and third immunoglobulin-like domains. The linker between domains 2
» and 3 appears to be flexible and is a critical determinant in maintaining
» an overall conformation for Lutheran that is capable of binding to Laminin.
» Mutagenesis studies indicate that Asp312 of Lutheran and the surrounding
» cluster of negatively charged residues in this linker region form the
» Laminin-binding site. Unusually, receptor binding is therefore not a
» function of the domains expected to be furthermost from the plasma
» membrane. These studies imply that structural flexibility of Lutheran may
» be essential for its interaction with Laminin and present a novel
» opportunity for the development of therapeutics for sickle cell disease.
»
»
»
»
» correct me if I am wrong, but is not Acell simply an extracellular matrix?
» if so it should contain this protein. what does this mean in regards to how
» Acell effects our hair follicles, I have no idea but hopefully it could
» help our struggle.

Now that is interesting, maybe someone with a medical perspective can clarify that aspect of Acell.

.


#7

» » The Laminin 511/521–binding site on the Lutheran blood group
» glycoprotein
» » is located at the flexible junction of Ig domains 2 and 3
» » Tosti J. Mankelow1, Nicholas Burton2, Fanney O. Stefansdottir1, Frances
» A.
» » Spring1, Stephen F. Parsons1, Jan S. Pedersen3, Cristiano L. P.
» Oliveira3,
» » Donna Lammie4, Timothy Wess4, Narla Mohandas5, Joel Anne Chasis6, R.
» Leo
» » Brady2, and David J. Anstee1
» »
» » 1 Bristol Institute for Transfusion Sciences (BITS), National Blood
» » Service, Bristol, United Kingdom; 2 Department of Biochemistry,
» University
» » of Bristol, Bristol, United Kingdom; 3 Department of Chemistry,
» University
» » of Aarhus, Aarhus, Denmark; 4 School of Optometry and Vision Sciences,
» » Cardiff University, Cardiff, United Kingdom; 5 New York Blood Center,
» New
» » York City; and 6 University of California, Lawrence Berkeley National
» » Laboratory, Berkeley
» »
» » The Lutheran blood group glycoprotein, first discovered on
» erythrocytes,
» » is widely expressed in human tissues. It is a ligand for the {alpha}5
» » subunit of Laminin 511/521, an extracellular
» matrix
» » protein. This interaction may contribute to
» vaso-occlusive
» » events that are an important cause of morbidity in sickle cell disease.
» » Using x-ray crystallography, small-angle x-ray scattering, and
» » site-directed mutagenesis, we show that the extracellular region of
» » Lutheran forms an extended structure with a distinctive bend between
» the
» » second and third immunoglobulin-like domains. The linker between domains
» 2
» » and 3 appears to be flexible and is a critical determinant in
» maintaining
» » an overall conformation for Lutheran that is capable of binding to
» Laminin.
» » Mutagenesis studies indicate that Asp312 of Lutheran and the
» surrounding
» » cluster of negatively charged residues in this linker region form the
» » Laminin-binding site. Unusually, receptor binding is therefore not a
» » function of the domains expected to be furthermost from the plasma
» » membrane. These studies imply that structural flexibility of Lutheran
» may
» » be essential for its interaction with Laminin and present a novel
» » opportunity for the development of therapeutics for sickle cell
» disease.
» »
» »
» »
» »
» » correct me if I am wrong, but is not Acell simply an extracellular
» matrix?
» » if so it should contain this protein. what does this mean in regards to
» how
» » Acell effects our hair follicles, I have no idea but hopefully it could
» » help our struggle.
»
» Now that is interesting, maybe someone with a medical perspective can
» clarify that aspect of Acell.
»
»
»
» .

yess very interesting mabye someone should try the acell thing see if it worksss… i mean mabye becuase of the fact that our bodies heal wounds so quickly our bodies dont have the chance to develope hairs… acell seems to keep the scabbing away so ur body can develope what was orriginally thier? just talking crap but it came to mind idk.


#8

Isn’t laminin a component of the ECM produced intracellularly by resident cells…

ECM (Acell) produces laminin at the site of the injury…

Whooo hooo WHHHHOOOOOOO HOOOOOO.

» Something to do with a molecule called laminin-511, and Dr. Cotsarelis
» chimes-in in the article. Unfortunately, it’s research merely at the mouse
» stage right now.
»
»
» http://www.mercurynews.com/breakingnews/ci_10058126?nclick_check=1
» By Vianna Davila
» Mercury News
» Article Launched: 07/31/2008 02:19:52 PM PDT
»
»
» Watch out, Rogaine.
» Stanford University researchers have pinpointed a molecule that triggers
» hair follicle growth in mice, a treatment that one day could eventually
» mean some shaggy dos, or at least a few more strands, for humans who have
» experienced hair loss.
»
» The report, published today in the Journal of Genes and Development,
» focuses on a molecule called laminin-511. The molecule acts like an
» operator, transferring messages, or proteins, between the outer and inner
» layers of skin, an exchange that ultimately drives hair formation.
»
» Unlike Rogaine or Propecia, products that slow hair loss, researchers hope
» the laminin-511 could potentially regenerate the actual follicles that grow
» hair.
»
» “Loss of hair is not going to kill anybody,” said Dr. Peter Marinkovich,
» the study’s senior author and an associate professor at Stanford
» University’s School of Medicine. “At the same time, for some people, hair
» loss can be a really traumatic thing, especially for women.”
»
» He hopes the treatment eventually could help patients who suffer from
» alopecia, a disorder that can cause hair loss in patches, or speed up hair
» growth for chemotherapy patients.
»
» Evidence suggests laminin-511 could lead to more than fuller heads of
» hair: researchers believe the molecule might have the ability to regenerate
» other developing tissues, like limbs or even organs; but further tests are
» necessary to understand exactly how that process works.
»
» In an earlier study using mice,
»
» Stanford researchers showed laminin-511 was essential for hair growth but
» they were unsure why. The recent study more clearly demonstrated how the
» molecule transfers signals within the skin in a way that particularly
» stimulates follicle growth. How soon did scientists see results? Mice
» injected with the purified molecule grew back hair in two weeks, at half
» the thickness of a normal rodent.
» But if you’re itching for a dose of laminin-511 to restore your once long
» locks, hold off on buying that bottle of hair gel - Do-It-Yourself
» treatments are likely years away.
»
» The Stanford study presents a new understanding of how laminin-511 works,
» said Dr. George Cotsarelis, director of the Hair and Scalp Clinic at the
» University of Pennsylvania School of Medicine. But more clinical trials are
» necessary to show how humans will react to the treatment.
»
» Marinkovich said his team hopes to repeat the tests on animals treated
» with chemotherapy and later on human subjects.
»
» The findings are “important in the long run,” Cotsarelis said, calling the
» Stanford study, “one of the initial steps.”
»
»
» Contact Vianna Davila at vdavila at mercurynews dot com or (408)
» 920-5064.
»
»
»
»
»
»
» .


#9

» » The Laminin 511/521–binding site on the Lutheran blood group
» glycoprotein
» » is located at the flexible junction of Ig domains 2 and 3
» » Tosti J. Mankelow1, Nicholas Burton2, Fanney O. Stefansdottir1, Frances
» A.
» » Spring1, Stephen F. Parsons1, Jan S. Pedersen3, Cristiano L. P.
» Oliveira3,
» » Donna Lammie4, Timothy Wess4, Narla Mohandas5, Joel Anne Chasis6, R.
» Leo
» » Brady2, and David J. Anstee1
» »
» » 1 Bristol Institute for Transfusion Sciences (BITS), National Blood
» » Service, Bristol, United Kingdom; 2 Department of Biochemistry,
» University
» » of Bristol, Bristol, United Kingdom; 3 Department of Chemistry,
» University
» » of Aarhus, Aarhus, Denmark; 4 School of Optometry and Vision Sciences,
» » Cardiff University, Cardiff, United Kingdom; 5 New York Blood Center,
» New
» » York City; and 6 University of California, Lawrence Berkeley National
» » Laboratory, Berkeley
» »
» » The Lutheran blood group glycoprotein, first discovered on
» erythrocytes,
» » is widely expressed in human tissues. It is a ligand for the {alpha}5
» » subunit of Laminin 511/521, an extracellular
» matrix
» » protein. This interaction may contribute to
» vaso-occlusive
» » events that are an important cause of morbidity in sickle cell disease.
» » Using x-ray crystallography, small-angle x-ray scattering, and
» » site-directed mutagenesis, we show that the extracellular region of
» » Lutheran forms an extended structure with a distinctive bend between
» the
» » second and third immunoglobulin-like domains. The linker between domains
» 2
» » and 3 appears to be flexible and is a critical determinant in
» maintaining
» » an overall conformation for Lutheran that is capable of binding to
» Laminin.
» » Mutagenesis studies indicate that Asp312 of Lutheran and the
» surrounding
» » cluster of negatively charged residues in this linker region form the
» » Laminin-binding site. Unusually, receptor binding is therefore not a
» » function of the domains expected to be furthermost from the plasma
» » membrane. These studies imply that structural flexibility of Lutheran
» may
» » be essential for its interaction with Laminin and present a novel
» » opportunity for the development of therapeutics for sickle cell
» disease.
» »
» »
» »
» »
» » correct me if I am wrong, but is not Acell simply an extracellular
» matrix?
» » if so it should contain this protein. what does this mean in regards to
» how
» » Acell effects our hair follicles, I have no idea but hopefully it could
» » help our struggle.
»
» Now that is interesting, maybe someone with a medical perspective can
» clarify that aspect of Acell.
»

Ok, someone here needs to get Acell asap because that actually makes good sense. All you would need to do is do a dermabrade of the outer tough skin to allow the acell powder to permeate the skin and in theory this stuff should work…


#10

It is interesting how extrodinarily complex the hair follicle cycle really is with all the little alphabet soup of chemicals that get secreted by the dermal papilla and cellular signals and prostaglandins and immuno cells that seemingly regulate it------------and the various alopecias where one or two things go wrong and stop the hair cycle from re-occuring or even causing an inflammatory alopecia that mars the skin around there…

Maybe this “go trigger” can get old hairs to shoot one more time and give someone a chance to get on a anti-androgen and save them…who knows. There are so many things seemingly involved in the hair cycle, Nitric Oxide, Potassium channels, prostaglandins, immuno cells, dermal papilla mitogens, dermal papilla antigens, dht, estrogn, testosterone, androstenidione…it really is incredible.

They have the tools now that can look “small enough” to see the tiny little things happening. Im hoping that at least one of these gives us the breakthrough we all want.


#11

It probably would be a good idea to send an email to the gentleman behind this stanford study, inform him about Acell and the fact that it might produce this molecule .His reaction might be interesting.

Also why not check if Oasis do contain this molecule or not !


#12

» It probably would be a good idea to send an email to the gentleman behind
» this stanford study, inform him about Acell and the fact that it might
» produce this molecule .His reaction might be interesting.
»
» Also why not check if Oasis do contain this molecule or not !

I think it’d be stupid not to.


#13

» It probably would be a good idea to send an email to the gentleman behind
» this stanford study, inform him about Acell and the fact that it might
» produce this molecule .His reaction might be interesting.
»
» Also why not check if Oasis do contain this molecule or not !

Man, wouldn’t it be nice if there was something readily available with that molecule.

.


#14

» It probably would be a good idea to send an email to the gentleman behind
» this stanford study, inform him about Acell and the fact that it might
» produce this molecule .His reaction might be interesting.
»
» Also why not check if Oasis do contain this molecule or not !

It would be sure tremendously nice to get our hands on this molecule with Acell !!!